Preparation of trisaccharides from alginate by a novel alginate lyase Alg7A from marine bacterium Vibrio sp. W13
Enzymatic digestion of sodium alginate to produce specific oligosaccharides has attracted great attention. However, commercial enzymes that efficiently produce specific oligosaccharides are still unavailable. In the present study, a novel gene encoding an alginate lyase (designated alg7A) was cloned...
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| Published in | International journal of biological macromolecules Vol. 139; pp. 879 - 885 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
15.10.2019
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| Online Access | Get full text |
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| Abstract | Enzymatic digestion of sodium alginate to produce specific oligosaccharides has attracted great attention. However, commercial enzymes that efficiently produce specific oligosaccharides are still unavailable. In the present study, a novel gene encoding an alginate lyase (designated alg7A) was cloned from the marine bacterium Vibrio sp. W13 and expressed in E. coli. The recombinant Alg7A shows high activities toward alginate, poly-α-l-guluronate (polyG), poly-β-d-mannuronate (polyM) and polyMG, and more preferred to polyMG. Moreover, the enzyme contains a highly conserved domain of the Polysaccharide Lyase (PL) 7 family (R*E*R, Q*H and Y*KAG*Y*Q), which indicates that it belongs to PL7. Furthermore, the thin layer chromatography and ESI-MS analysis showed that Alg7A mainly releases trisaccharides from alginate. These results demonstrated that Alg7A has a great potential to be used to produce oligosaccharides from alginate.
•Trisaccharides can be mainly produced from alginate by a novel alginate lyase Alg7A with high activity and broad substrate specificity.•Alg7A is a bifunctional lyase toward both polyG and polyM.•These characteristics demonstrated that its potential application in the production of oligosaccharides with low polymerization degrees. |
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| AbstractList | Enzymatic digestion of sodium alginate to produce specific oligosaccharides has attracted great attention. However, commercial enzymes that efficiently produce specific oligosaccharides are still unavailable. In the present study, a novel gene encoding an alginate lyase (designated alg7A) was cloned from the marine bacterium Vibrio sp. W13 and expressed in E. coli. The recombinant Alg7A shows high activities toward alginate, poly-α-l-guluronate (polyG), poly-β-d-mannuronate (polyM) and polyMG, and more preferred to polyMG. Moreover, the enzyme contains a highly conserved domain of the Polysaccharide Lyase (PL) 7 family (R*E*R, Q*H and Y*KAG*Y*Q), which indicates that it belongs to PL7. Furthermore, the thin layer chromatography and ESI-MS analysis showed that Alg7A mainly releases trisaccharides from alginate. These results demonstrated that Alg7A has a great potential to be used to produce oligosaccharides from alginate.
•Trisaccharides can be mainly produced from alginate by a novel alginate lyase Alg7A with high activity and broad substrate specificity.•Alg7A is a bifunctional lyase toward both polyG and polyM.•These characteristics demonstrated that its potential application in the production of oligosaccharides with low polymerization degrees. Enzymatic digestion of sodium alginate to produce specific oligosaccharides has attracted great attention. However, commercial enzymes that efficiently produce specific oligosaccharides are still unavailable. In the present study, a novel gene encoding an alginate lyase (designated alg7A) was cloned from the marine bacterium Vibrio sp. W13 and expressed in E. coli. The recombinant Alg7A shows high activities toward alginate, poly-α-l-guluronate (polyG), poly-β-d-mannuronate (polyM) and polyMG, and more preferred to polyMG. Moreover, the enzyme contains a highly conserved domain of the Polysaccharide Lyase (PL) 7 family (R*E*R, Q*H and Y*KAG*Y*Q), which indicates that it belongs to PL7. Furthermore, the thin layer chromatography and ESI-MS analysis showed that Alg7A mainly releases trisaccharides from alginate. These results demonstrated that Alg7A has a great potential to be used to produce oligosaccharides from alginate. |
| Author | Ning, Limin Zhao, Xiaoming Wang, Wenxia Yin, Heng Li, Kuikui Tan, Haidong Zhu, Benwei |
| Author_xml | – sequence: 1 givenname: Benwei surname: Zhu fullname: Zhu, Benwei organization: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, CAS, Dalian 116023, China – sequence: 2 givenname: Kuikui surname: Li fullname: Li, Kuikui organization: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, CAS, Dalian 116023, China – sequence: 3 givenname: Wenxia surname: Wang fullname: Wang, Wenxia organization: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, CAS, Dalian 116023, China – sequence: 4 givenname: Limin surname: Ning fullname: Ning, Limin organization: Preclinical Medicine College, Nanjing University of Chinese Medicine, Nanjing 210023, China – sequence: 5 givenname: Haidong surname: Tan fullname: Tan, Haidong organization: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, CAS, Dalian 116023, China – sequence: 6 givenname: Xiaoming surname: Zhao fullname: Zhao, Xiaoming organization: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, CAS, Dalian 116023, China – sequence: 7 givenname: Heng surname: Yin fullname: Yin, Heng email: yinheng@dicp.ac.cn organization: Dalian Engineering Research Center for Carbohydrate Agricultural Preparations, Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, CAS, Dalian 116023, China |
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| Cites_doi | 10.1016/j.bbagen.2018.05.024 10.1016/j.jmb.2003.12.071 10.1016/0922-338X(93)90040-F 10.1039/C7CC06523J 10.1107/S090744491202495X 10.1016/S0008-6215(99)00062-2 10.1016/j.foodhyd.2018.03.053 10.1016/j.algal.2016.03.008 10.1016/j.jmb.2008.05.008 10.1074/jbc.M115.713230 10.1016/j.micres.2015.09.004 10.1016/j.foodchem.2018.07.026 10.1111/j.1574-6968.1999.tb08776.x 10.1016/j.ijbiomac.2015.01.053 10.3389/fmicb.2016.01120 10.1016/j.carres.2012.05.019 10.1038/s41598-017-13288-1 10.1016/j.progpolymsci.2011.06.003 10.1006/jmbi.1999.2883 10.1016/j.carbpol.2013.07.050 10.1271/bbb.67.258 10.1111/j.1574-6968.1993.tb06302.x 10.1042/bj3190575 10.1016/j.ijbiomac.2017.10.164 10.1007/s10811-011-9679-y 10.1007/s10529-012-0876-9 10.1006/jmbi.2000.4509 10.1016/S1570-9639(03)00105-5 10.1016/S1389-1723(00)88738-1 10.3390/md16090295 10.1016/j.biochi.2011.06.004 10.3389/fphar.2017.00623 10.1271/bbb.64.1067 10.1016/j.enzmictec.2007.07.003 10.1128/JB.182.16.4572-4577.2000 10.1007/s10126-005-6157-z 10.1007/s00792-008-0201-7 10.1146/annurev.micro.54.1.289 10.1007/s002840010182 10.1016/0020-711X(92)90325-U 10.1016/j.jmb.2005.06.075 10.1002/bab.1506 10.1016/j.carres.2003.08.009 10.1007/s10295-012-1210-1 10.1128/AEM.58.8.2474-2478.1992 10.1007/s10126-009-9237-7 10.1002/cpbi.3 10.1016/j.foodhyd.2018.03.056 10.3389/fmicb.2018.02894 10.1016/j.jmb.2005.05.055 10.1002/jcc.21256 10.3390/md14060108 10.2174/09298665113206660094 10.1007/s10126-011-9402-7 10.1006/viro.2000.0590 10.1007/s13197-018-3101-6 |
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| Keywords | Alginate oligosaccharides Alginate lyase Trisaccharide |
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| References | Iwasaki, Matsubara (bb0040) 2000; 64 Qin, Miyakawa, Inoue, Nishiyama, Nakamura, Asano, Ojima, Tanokura (bb0145) 2018; 54 Kim, Ko, Kim, Kim, Lee, Choi, Woo, Kim, Kim (bb0265) 2012; 34 Chen, Dong, Xu, Dong, Li, Zhang, Zhou, Zhang, Xie (bb0165) 2016; 7 Chen, Hu, Zhang, Wang, Wang, Zhang, Guo, Ji, Wang (bb0130) 2017; 8 Zhu, Sun, Ni, Ning, Yao (bb0255) 2018; 108 Park, Kam, Lee, Kim (bb0210) 2012; 14 Hifney, Fawzy, Abdel-Gawad, Gomaa (bb0055) 2018; 269 Rahman, Inoue, Tanaka, Ojima (bb0070) 2011; 93 Chavagnat, Duez, Guinand, Potin, Barbeyron, Henrissat, Wallach, Ghuyse (bb0095) 1996; 319 Inoue, Anraku, Nakagawa, Ojima (bb0100) 2016; 291 Gacesa (bb0010) 1992; 24 Rahman, Wang, Inoue, Ojima (bb0080) 2012; 360 Inoue, Nishiyama, Ojima (bb0105) 2016; 19 Zhu, Chen, Yin, Du, Ning (bb0110) 2016; 14 Sugimoto, Hiramatsu, Murakami, Fujie, Usami, Yamada (bb0125) 2000; 277 Uchimura, Miyazaki, Nogi, Kobayashi, Horikoshi (bb0175) 2010; 12 Zhu, Wu, Chen, Ni, Xiao, Cai (bb0270) 2016; 182 Zhao, Li, Xue, Sun (bb0050) 2012; 24 Shimizu, Ojima, Nishita (bb0075) 2003; 338 Suda, Tanji, Hori, Unno (bb0120) 1999; 180 Yang, Yu, Yang, Shi, Mou, Li (bb0235) 2018; 9 Stephen, Phillips, Williams (bb0005) 2006 Sim, Furusawa, Teh (bb0065) 2017; 7 Wong, Preston, Schiller (bb0060) 2000; 54 Maruyama, Hashimoto, Mikami, Murata (bb0295) 2005; 350 Malissard, Duez, Guinand, Vacheron, Michel, Marty, Joris, Thamm, Ghuysen (bb0185) 1993; 110 Huang, Zhou, Li, Peng, Lu, Du (bb0260) 2013; 40 Zhuang, Zhang, Liu, Liu, Lyu, Ji (bb0230) 2018; 16 Gong, Liu, Zhang, Li, Geng, Li, Li, Lu, Xu, Shi (bb0115) 2017; 64 Kobayashi, Uchimura, Miyazaki, Nogi, Horikoshi (bb0200) 2009; 13 Kawamoto, Horibe, Miki, Kimura, Tanaka, Nakagawa, Kawamukai, Matsuda (bb0180) 2006; 8 Ott, Day, Koenig, Pierson (bb0150) 2001; 42 Inoue, Nishiyama, Ojima (bb0085) 2016 Matsubara, Kawada, Iwasaki, Kimura, Oda, Muramatsu (bb0190) 2000; 89 Peng, Zhang, Gao, Eromosele, Qiao, Shi (bb0135) 2018; 55 Yoon, Mikami, Hashimoto, Murata (bb0240) 1999; 290 Gomaa, Fawzy, Hifney, Abdel-Gawad (bb0020) 2018; 82 Yoon, Hashimoto, Miyake, Murata, Mikami (bb0285) 2001; 307 Deng, Ye, Xu, Zhang (bb0170) 2014; 21 Ogura, Yamasaki, Mikami, Hashimoto, Murata (bb0250) 2008; 380 Lee, Mooney (bb0030) 2012; 37 Webb, Sali (bb0155) 2016; 54 Song, Yu, Han, Han, Li (bb0225) 2003; 35 Mikami, Ban, Suzuki, Yoon, Miyake, Yamasaki, Ogura, Maruyama, Hashimoto, Murata (bb0280) 2012; 68 Gomaa, Hifney, Fawzy, Abdel-Gawad (bb0025) 2018; 82 Yang, Qin, Lehotay, Toki, Dennis, Schutzbach, Brockhausen (bb0245) 2003; 1648 Zhu, Tan, Qin, Xu, Du, Yin (bb0090) 2015; 75 Lyu, Zhang, Zhu, Li, Liu, Fitzek, Yohe, Zhao, Li, Liu, Yin, Liu (bb0140) 2018; 1862 Fu, Lin, Kim (bb0215) 2007; 41 Murata, Inose, Hisano, Abe, Yonemoto, Yamashita, Takagi, Sakaguchi, Kimura, Imanaka (bb0035) 1993; 76 Dou, Wei, Li, Li, Rahman, Shi, Xu, Ma (bb0205) 2013; 98 Morris, Huey, Lindstrom, Sanner, Belew, Goodsell, Olson (bb0160) 2009; 30 Yamasaki, Ogura, Hashimoto, Mikami, Murata (bb0275) 2005; 352 Hashimoto, Miyake, Momma, Kawai, Murata (bb0195) 2000; 182 Braccini, Grasso, Perez (bb0015) 1999; 317 Iwamoto, Xu, Tamura, Oda, Muramatsu (bb0045) 2003; 67 Lunin, Li, Linhardt, Miyazono, Kyogashima, Kaneko, Bell, Cygler (bb0290) 2004; 337 Kitamikado, Tseng, Yamaguchi, Nakamura (bb0220) 1992; 58 Hashimoto (10.1016/j.ijbiomac.2019.08.020_bb0195) 2000; 182 Gacesa (10.1016/j.ijbiomac.2019.08.020_bb0010) 1992; 24 Morris (10.1016/j.ijbiomac.2019.08.020_bb0160) 2009; 30 Chen (10.1016/j.ijbiomac.2019.08.020_bb0165) 2016; 7 Sugimoto (10.1016/j.ijbiomac.2019.08.020_bb0125) 2000; 277 Yoon (10.1016/j.ijbiomac.2019.08.020_bb0285) 2001; 307 Shimizu (10.1016/j.ijbiomac.2019.08.020_bb0075) 2003; 338 Sim (10.1016/j.ijbiomac.2019.08.020_bb0065) 2017; 7 Qin (10.1016/j.ijbiomac.2019.08.020_bb0145) 2018; 54 Lee (10.1016/j.ijbiomac.2019.08.020_bb0030) 2012; 37 Iwasaki (10.1016/j.ijbiomac.2019.08.020_bb0040) 2000; 64 Park (10.1016/j.ijbiomac.2019.08.020_bb0210) 2012; 14 Chen (10.1016/j.ijbiomac.2019.08.020_bb0130) 2017; 8 Zhuang (10.1016/j.ijbiomac.2019.08.020_bb0230) 2018; 16 Zhao (10.1016/j.ijbiomac.2019.08.020_bb0050) 2012; 24 Braccini (10.1016/j.ijbiomac.2019.08.020_bb0015) 1999; 317 Maruyama (10.1016/j.ijbiomac.2019.08.020_bb0295) 2005; 350 Inoue (10.1016/j.ijbiomac.2019.08.020_bb0105) 2016; 19 Huang (10.1016/j.ijbiomac.2019.08.020_bb0260) 2013; 40 Yoon (10.1016/j.ijbiomac.2019.08.020_bb0240) 1999; 290 Deng (10.1016/j.ijbiomac.2019.08.020_bb0170) 2014; 21 Iwamoto (10.1016/j.ijbiomac.2019.08.020_bb0045) 2003; 67 Zhu (10.1016/j.ijbiomac.2019.08.020_bb0110) 2016; 14 Malissard (10.1016/j.ijbiomac.2019.08.020_bb0185) 1993; 110 Matsubara (10.1016/j.ijbiomac.2019.08.020_bb0190) 2000; 89 Stephen (10.1016/j.ijbiomac.2019.08.020_bb0005) 2006 Kobayashi (10.1016/j.ijbiomac.2019.08.020_bb0200) 2009; 13 Gomaa (10.1016/j.ijbiomac.2019.08.020_bb0020) 2018; 82 Lyu (10.1016/j.ijbiomac.2019.08.020_bb0140) 2018; 1862 Dou (10.1016/j.ijbiomac.2019.08.020_bb0205) 2013; 98 Ott (10.1016/j.ijbiomac.2019.08.020_bb0150) 2001; 42 Webb (10.1016/j.ijbiomac.2019.08.020_bb0155) 2016; 54 Yamasaki (10.1016/j.ijbiomac.2019.08.020_bb0275) 2005; 352 Hifney (10.1016/j.ijbiomac.2019.08.020_bb0055) 2018; 269 Gong (10.1016/j.ijbiomac.2019.08.020_bb0115) 2017; 64 Murata (10.1016/j.ijbiomac.2019.08.020_bb0035) 1993; 76 Zhu (10.1016/j.ijbiomac.2019.08.020_bb0090) 2015; 75 Kawamoto (10.1016/j.ijbiomac.2019.08.020_bb0180) 2006; 8 Yang (10.1016/j.ijbiomac.2019.08.020_bb0235) 2018; 9 Peng (10.1016/j.ijbiomac.2019.08.020_bb0135) 2018; 55 Inoue (10.1016/j.ijbiomac.2019.08.020_bb0085) 2016 Yang (10.1016/j.ijbiomac.2019.08.020_bb0245) 2003; 1648 Rahman (10.1016/j.ijbiomac.2019.08.020_bb0070) 2011; 93 Kitamikado (10.1016/j.ijbiomac.2019.08.020_bb0220) 1992; 58 Ogura (10.1016/j.ijbiomac.2019.08.020_bb0250) 2008; 380 Suda (10.1016/j.ijbiomac.2019.08.020_bb0120) 1999; 180 Zhu (10.1016/j.ijbiomac.2019.08.020_bb0255) 2018; 108 Kim (10.1016/j.ijbiomac.2019.08.020_bb0265) 2012; 34 Fu (10.1016/j.ijbiomac.2019.08.020_bb0215) 2007; 41 Mikami (10.1016/j.ijbiomac.2019.08.020_bb0280) 2012; 68 Chavagnat (10.1016/j.ijbiomac.2019.08.020_bb0095) 1996; 319 Song (10.1016/j.ijbiomac.2019.08.020_bb0225) 2003; 35 Gomaa (10.1016/j.ijbiomac.2019.08.020_bb0025) 2018; 82 Lunin (10.1016/j.ijbiomac.2019.08.020_bb0290) 2004; 337 Inoue (10.1016/j.ijbiomac.2019.08.020_bb0100) 2016; 291 Wong (10.1016/j.ijbiomac.2019.08.020_bb0060) 2000; 54 Uchimura (10.1016/j.ijbiomac.2019.08.020_bb0175) 2010; 12 Zhu (10.1016/j.ijbiomac.2019.08.020_bb0270) 2016; 182 Rahman (10.1016/j.ijbiomac.2019.08.020_bb0080) 2012; 360 |
| References_xml | – volume: 67 start-page: 258 year: 2003 end-page: 263 ident: bb0045 article-title: Enzymatically depolymerized alginate oligomers that cause cytotoxic cytokine production in human mononuclear cells publication-title: Biosci. Biotechnol. Biochem. contributor: fullname: Muramatsu – volume: 30 start-page: 2785 year: 2009 end-page: 2791 ident: bb0160 article-title: AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility publication-title: J. Comput. Chem. contributor: fullname: Olson – volume: 350 start-page: 974 year: 2005 end-page: 986 ident: bb0295 article-title: Crystal structure of Bacillus sp GL1 xanthan lyase complexed with a substrate: insights into the enzyme reaction mechanism publication-title: J. Mol. Biol. contributor: fullname: Murata – volume: 14 start-page: 189 year: 2012 end-page: 202 ident: bb0210 article-title: Cloning and characterization of a novel oligoalginate lyase from a newly isolated bacterium Sphingomonas sp. MJ-3 publication-title: Mar. Biotechnol. contributor: fullname: Kim – volume: 16 start-page: 1 year: 2018 end-page: 12 ident: bb0230 article-title: Characterization of a novel PolyM-preferred alginate lyase from marine Vibrio splendidus OU02 publication-title: Mar. Drugs contributor: fullname: Ji – volume: 180 start-page: 45 year: 1999 end-page: 53 ident: bb0120 article-title: Evidence for a novel Chlorella virus-encoded alginate lyase publication-title: FEMS Microbiol. Lett. contributor: fullname: Unno – volume: 54 start-page: 5.6.1 year: 2016 end-page: 5.6.37 ident: bb0155 article-title: Comparative protein structure modeling using MODELLER publication-title: Curr. Protoc. Bioinformatics contributor: fullname: Sali – volume: 380 start-page: 373 year: 2008 end-page: 385 ident: bb0250 article-title: Substrate recognition by family 7 alginate lyase from Sphingomonas sp A1 publication-title: J. Mol. Biol. contributor: fullname: Murata – volume: 24 start-page: 545 year: 1992 end-page: 552 ident: bb0010 article-title: Enzymic degradation of alginates publication-title: Int. J. Biochem. contributor: fullname: Gacesa – volume: 21 start-page: 179 year: 2014 end-page: 187 ident: bb0170 article-title: Structural and functional studies on three alginate lyases from Vibrio alginolyticus publication-title: Protein Pept Lett contributor: fullname: Zhang – volume: 8 start-page: 481 year: 2006 end-page: 490 ident: bb0180 article-title: Cloning and sequencing analysis of alginate lyase genes from the marine bacterium Vibrio sp. O2 publication-title: Mar. Biotechnol. contributor: fullname: Matsuda – volume: 7 start-page: 1 year: 2017 end-page: 9 ident: bb0065 article-title: Functional and structural studies of a multidomain alginate Lyase from Persicobacter sp. CCB-QB2 publication-title: Sci. Rep. contributor: fullname: Teh – volume: 9 start-page: 1 year: 2018 end-page: 13 ident: bb0235 article-title: Expression and characterization of a new PolyG-specific alginate lyase from marine bacterium Microbulbifer sp Q7 publication-title: Front. Microbiol. contributor: fullname: Li – volume: 37 start-page: 106 year: 2012 end-page: 126 ident: bb0030 article-title: Alginate: properties and biomedical applications publication-title: Prog. Polym. Sci. contributor: fullname: Mooney – volume: 98 start-page: 1476 year: 2013 end-page: 1482 ident: bb0205 article-title: Purification and characterisation of a bifunctional alginate lyase from novel Isoptericola halotolerans CGMCC 5336 publication-title: Carbohydr. Polym. contributor: fullname: Ma – volume: 34 start-page: 1087 year: 2012 end-page: 1092 ident: bb0265 article-title: Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans publication-title: Biotechnol. Lett. contributor: fullname: Kim – volume: 7 start-page: 1 year: 2016 end-page: 9 ident: bb0165 article-title: Characterization of a new cold-adapted and salt-activated polysaccharide lyase family 7 alginate lyase from Pseudoalteromonas sp. SM0524 publication-title: Front. Microbiol. contributor: fullname: Xie – volume: 41 start-page: 828 year: 2007 end-page: 834 ident: bb0215 article-title: Purification and characterization of a Na+/K+ dependent alginate lyase from turban shell gut Vibrio sp. YKW-34 publication-title: Enzym. Microb. Technol. contributor: fullname: Kim – volume: 317 start-page: 119 year: 1999 end-page: 130 ident: bb0015 article-title: Conformational and configurational features of acidic polysaccharides and their interactions with calcium ions: a molecular modeling investigation publication-title: Carbohydr. Res. contributor: fullname: Perez – volume: 54 start-page: 289 year: 2000 end-page: 340 ident: bb0060 article-title: ALGINATE LYASE: review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications publication-title: Annu. Rev. Microbiol. contributor: fullname: Schiller – volume: 277 start-page: 119 year: 2000 end-page: 126 ident: bb0125 article-title: Algal-lytic activities encoded by Chlorella virus CVK2 publication-title: Virology contributor: fullname: Yamada – volume: 110 start-page: 101 year: 1993 end-page: 106 ident: bb0185 article-title: Sequence of a gene encoding a (poly mana) alginate lyase active on pseudomonas-aeruginosa alginate publication-title: FEMS Microbiol. Lett. contributor: fullname: Ghuysen – volume: 40 start-page: 113 year: 2013 end-page: 122 ident: bb0260 article-title: Characterization of a new alginate lyase from newly isolated Flavobacterium sp S20 publication-title: J. Ind. Microbiol. Biotechnol. contributor: fullname: Du – volume: 13 start-page: 121 year: 2009 end-page: 129 ident: bb0200 article-title: A new high-alkaline alginate lyase from a deep-sea bacterium Agarivorans sp publication-title: Extremophiles contributor: fullname: Horikoshi – volume: 35 start-page: 473 year: 2003 end-page: 477 ident: bb0225 article-title: Purification and characterization of aginate lyase from marine bacterium Vibrio sp. QY101 publication-title: Acta Biochim. Biophys. Sin. contributor: fullname: Li – volume: 24 start-page: 295 year: 2012 end-page: 300 ident: bb0050 article-title: Effect of molecular weight on the antioxidant property of low molecular weight alginate from Laminaria japonica publication-title: J. Appl. Phycol. contributor: fullname: Sun – volume: 42 start-page: 78 year: 2001 end-page: 81 ident: bb0150 article-title: The release of alginate lyase from growing Pseudomonas syringae pathovar phaseolicola publication-title: Curr. Microbiol. contributor: fullname: Pierson – volume: 307 start-page: 9 year: 2001 end-page: 16 ident: bb0285 article-title: Crystal structure of alginate lyase A1-III complexed with trisaccharide product at 2.0 angstrom resolution publication-title: J. Mol. Biol. contributor: fullname: Mikami – volume: 68 start-page: 1207 year: 2012 end-page: 1216 ident: bb0280 article-title: Induced-fit motion of a lid loop involved in catalysis in alginate lyase A1-III publication-title: Acta Crystallogr. D Biol. Crystallogr. contributor: fullname: Murata – volume: 290 start-page: 505 year: 1999 end-page: 514 ident: bb0240 article-title: Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 angstrom resolution publication-title: J. Mol. Biol. contributor: fullname: Murata – volume: 19 start-page: 355 year: 2016 end-page: 362 ident: bb0105 article-title: The alginate lyases FlAlyA, FlAlyB, FlAlyC, and FlAlex from Flavobacterium sp UMI-01 have distinct roles in the complete degradation of alginate publication-title: Algal Res. contributor: fullname: Ojima – volume: 360 start-page: 69 year: 2012 end-page: 77 ident: bb0080 article-title: cDNA cloning and bacterial expression of a PL-14 alginate lyase from a herbivorous marine snail Littorina brevicula publication-title: Carbohydr. Res. contributor: fullname: Ojima – volume: 76 start-page: 427 year: 1993 end-page: 437 ident: bb0035 article-title: Bacterial alginate lyase - enzymology, genetics and application publication-title: J. Ferment. Bioeng. contributor: fullname: Imanaka – volume: 182 start-page: 4572 year: 2000 end-page: 4577 ident: bb0195 article-title: Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate publication-title: J. Bacteriol. contributor: fullname: Murata – volume: 89 start-page: 199 year: 2000 end-page: 202 ident: bb0190 article-title: Cloning and sequence analysis of a gene (aly PG) encoding poly(alpha-L-guluronate)lyase from Corynebacterium sp. strain ALY-1 publication-title: J. Biosci. Bioeng. contributor: fullname: Muramatsu – volume: 1862 start-page: 1862 year: 2018 end-page: 1869 ident: bb0140 article-title: Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes publication-title: Biochim. Biophys. Acta Gen. Subj. contributor: fullname: Liu – volume: 337 start-page: 367 year: 2004 end-page: 386 ident: bb0290 article-title: High-resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: an enzyme-substrate complex defines the catalytic mechanism publication-title: J. Mol. Biol. contributor: fullname: Cygler – volume: 64 start-page: 1067 year: 2000 end-page: 1070 ident: bb0040 article-title: Purification of alginate oligosaccharides with root growth-promoting activity toward lettuce publication-title: Biosci. Biotechnol. Biochem. contributor: fullname: Matsubara – volume: 269 start-page: 387 year: 2018 end-page: 395 ident: bb0055 article-title: Upgrading the antioxidant properties of fucoidan and alginate from Cystoseira trinodis by fungal fermentation or enzymatic pretreatment of the seaweed biomass publication-title: Food Chem. contributor: fullname: Gomaa – volume: 338 start-page: 2841 year: 2003 end-page: 2852 ident: bb0075 article-title: cDNA cloning of an alginate lyase from abalone, Haliotis discus hannai publication-title: Carbohydr. Res. contributor: fullname: Nishita – volume: 54 start-page: 555 year: 2018 end-page: 558 ident: bb0145 article-title: Structural basis for controlling the enzymatic properties of polymannuronate preferred alginate lyase FlAlyA from the PL-7 family publication-title: Chem. Commun. contributor: fullname: Tanokura – volume: 55 start-page: 1850 year: 2018 end-page: 1858 ident: bb0135 article-title: Effects of alginate oligosaccharides with different molecular weights and guluronic to mannuronic acid ratios on glyceollin induction and accumulation in soybeans publication-title: J. Food Sci. Technol. contributor: fullname: Shi – volume: 352 start-page: 11 year: 2005 end-page: 21 ident: bb0275 article-title: A structural basis for depolymerization of alginate by polysaccharide lyase family-7 publication-title: J. Mol. Biol. contributor: fullname: Murata – volume: 64 start-page: 519 year: 2017 end-page: 524 ident: bb0115 article-title: Purification and characterization of a high salt-tolerant alginate lyase from Cobetia sp WG-007 publication-title: Biotechnol. Appl. Biochem. contributor: fullname: Shi – volume: 12 start-page: 526 year: 2010 end-page: 533 ident: bb0175 article-title: Cloning and sequencing of alginate lyase genes from deep-sea strains of Vibrio and Agarivorans and characterization of a new Vibrio enzyme publication-title: Mar. Biotechnol. contributor: fullname: Horikoshi – volume: 182 start-page: 49 year: 2016 end-page: 58 ident: bb0270 article-title: Characterization of an extracellular biofunctional alginate lyase from marine Microbulbifer sp ALW1 and antioxidant activity of enzymatic hydrolysates publication-title: Microbiol. Res. contributor: fullname: Cai – year: 2006 ident: bb0005 article-title: Food Polysaccharides and their Applications contributor: fullname: Williams – volume: 14 start-page: 2 year: 2016 end-page: 11 ident: bb0110 article-title: Enzymatic hydrolysis of alginate to produce oligosaccharides by a new purified Endo-type alginate lyase publication-title: Mar. Drugs contributor: fullname: Ning – volume: 108 start-page: 1140 year: 2018 end-page: 1147 ident: bb0255 article-title: Characterization of a new endo-type alginate lyase from Vibrio sp NJU-03 publication-title: Int. J. Biol. Macromol. contributor: fullname: Yao – volume: 1648 start-page: 62 year: 2003 end-page: 74 ident: bb0245 article-title: Soluble human core 2 beta 6-N-acetylglucosaminyltransferase C2GnT1 requires its conserved cysteine residues for full activity publication-title: Biochim. Biophys Acta-Proteins Proteomics contributor: fullname: Brockhausen – volume: 58 start-page: 2474 year: 1992 end-page: 2478 ident: bb0220 article-title: Two types of bacterial alginate lyases publication-title: Appl. Environ. Microbiol. contributor: fullname: Nakamura – volume: 291 start-page: 15551 year: 2016 end-page: 15563 ident: bb0100 article-title: Discovery of a novel alginate lyase from Nitratiruptor sp SB155-2 thriving at deep-sea hydrothermal vents and identification of the residues responsible for its heat stability publication-title: J. Biol. Chem. contributor: fullname: Ojima – volume: 82 start-page: 64 year: 2018 end-page: 72 ident: bb0020 article-title: Use of the brown seaweed Sargassum latifolium in the design of alginate-fucoidan based films with natural antioxidant properties and kinetic modeling of moisture sorption and polyphenolic release publication-title: Food Hydrocoll. contributor: fullname: Abdel-Gawad – volume: 82 start-page: 239 year: 2018 end-page: 247 ident: bb0025 article-title: Use of seaweed and filamentous fungus derived polysaccharides in the development of alginate-chitosan edible films containing fucoidan: study of moisture sorption, polyphenol release and antioxidant properties publication-title: Food Hydrocoll. contributor: fullname: Abdel-Gawad – volume: 8 start-page: 1 year: 2017 end-page: 11 ident: bb0130 article-title: Alginate oligosaccharide DP5 exhibits antitumor effects in osteosarcoma patients following surgery publication-title: Front. Pharmacol. contributor: fullname: Wang – volume: 75 start-page: 330 year: 2015 end-page: 337 ident: bb0090 article-title: Characterization of a new endo-type alginate lyase from Vibrio sp W13 publication-title: Int. J. Biol. Macromol. contributor: fullname: Yin – volume: 319 start-page: 575 year: 1996 end-page: 583 ident: bb0095 article-title: Cloning, sequencing and overexpression in Escherichia coli of the alginate lyase-encoding aly gene of pseudomonas alginovora: identification of three classes of alginate lyases publication-title: Biochem. J. contributor: fullname: Ghuyse – start-page: 355 year: 2016 end-page: 362 ident: bb0085 article-title: The alginate lyases FlAlyA, FlAlyB, FlAlyC, and FlAlex from Flavobacterium sp. UMI-01 have distinct roles in the complete degradation of alginate publication-title: Algal Res. contributor: fullname: Ojima – volume: 93 start-page: 1720 year: 2011 end-page: 1730 ident: bb0070 article-title: cDNA cloning of an alginate lyase from a marine gastropod Aplysia kurodai and assessment of catalytically important residues of this enzyme publication-title: Biochimie contributor: fullname: Ojima – volume: 1862 start-page: 1862 issue: 9 year: 2018 ident: 10.1016/j.ijbiomac.2019.08.020_bb0140 article-title: Structural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes publication-title: Biochim. Biophys. Acta Gen. Subj. doi: 10.1016/j.bbagen.2018.05.024 contributor: fullname: Lyu – volume: 337 start-page: 367 issue: 2 year: 2004 ident: 10.1016/j.ijbiomac.2019.08.020_bb0290 article-title: High-resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: an enzyme-substrate complex defines the catalytic mechanism publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2003.12.071 contributor: fullname: Lunin – volume: 76 start-page: 427 issue: 5 year: 1993 ident: 10.1016/j.ijbiomac.2019.08.020_bb0035 article-title: Bacterial alginate lyase - enzymology, genetics and application publication-title: J. Ferment. Bioeng. doi: 10.1016/0922-338X(93)90040-F contributor: fullname: Murata – volume: 54 start-page: 555 issue: 5 year: 2018 ident: 10.1016/j.ijbiomac.2019.08.020_bb0145 article-title: Structural basis for controlling the enzymatic properties of polymannuronate preferred alginate lyase FlAlyA from the PL-7 family publication-title: Chem. Commun. doi: 10.1039/C7CC06523J contributor: fullname: Qin – volume: 68 start-page: 1207 year: 2012 ident: 10.1016/j.ijbiomac.2019.08.020_bb0280 article-title: Induced-fit motion of a lid loop involved in catalysis in alginate lyase A1-III publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S090744491202495X contributor: fullname: Mikami – volume: 317 start-page: 119 issue: 1–4 year: 1999 ident: 10.1016/j.ijbiomac.2019.08.020_bb0015 article-title: Conformational and configurational features of acidic polysaccharides and their interactions with calcium ions: a molecular modeling investigation publication-title: Carbohydr. Res. doi: 10.1016/S0008-6215(99)00062-2 contributor: fullname: Braccini – volume: 82 start-page: 64 year: 2018 ident: 10.1016/j.ijbiomac.2019.08.020_bb0020 article-title: Use of the brown seaweed Sargassum latifolium in the design of alginate-fucoidan based films with natural antioxidant properties and kinetic modeling of moisture sorption and polyphenolic release publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2018.03.053 contributor: fullname: Gomaa – start-page: 355 year: 2016 ident: 10.1016/j.ijbiomac.2019.08.020_bb0085 article-title: The alginate lyases FlAlyA, FlAlyB, FlAlyC, and FlAlex from Flavobacterium sp. UMI-01 have distinct roles in the complete degradation of alginate publication-title: Algal Res. doi: 10.1016/j.algal.2016.03.008 contributor: fullname: Inoue – volume: 380 start-page: 373 issue: 2 year: 2008 ident: 10.1016/j.ijbiomac.2019.08.020_bb0250 article-title: Substrate recognition by family 7 alginate lyase from Sphingomonas sp A1 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2008.05.008 contributor: fullname: Ogura – volume: 291 start-page: 15551 issue: 30 year: 2016 ident: 10.1016/j.ijbiomac.2019.08.020_bb0100 article-title: Discovery of a novel alginate lyase from Nitratiruptor sp SB155-2 thriving at deep-sea hydrothermal vents and identification of the residues responsible for its heat stability publication-title: J. Biol. Chem. doi: 10.1074/jbc.M115.713230 contributor: fullname: Inoue – volume: 182 start-page: 49 year: 2016 ident: 10.1016/j.ijbiomac.2019.08.020_bb0270 article-title: Characterization of an extracellular biofunctional alginate lyase from marine Microbulbifer sp ALW1 and antioxidant activity of enzymatic hydrolysates publication-title: Microbiol. Res. doi: 10.1016/j.micres.2015.09.004 contributor: fullname: Zhu – volume: 269 start-page: 387 year: 2018 ident: 10.1016/j.ijbiomac.2019.08.020_bb0055 article-title: Upgrading the antioxidant properties of fucoidan and alginate from Cystoseira trinodis by fungal fermentation or enzymatic pretreatment of the seaweed biomass publication-title: Food Chem. doi: 10.1016/j.foodchem.2018.07.026 contributor: fullname: Hifney – volume: 180 start-page: 45 issue: 1 year: 1999 ident: 10.1016/j.ijbiomac.2019.08.020_bb0120 article-title: Evidence for a novel Chlorella virus-encoded alginate lyase publication-title: FEMS Microbiol. Lett. doi: 10.1111/j.1574-6968.1999.tb08776.x contributor: fullname: Suda – volume: 75 start-page: 330 year: 2015 ident: 10.1016/j.ijbiomac.2019.08.020_bb0090 article-title: Characterization of a new endo-type alginate lyase from Vibrio sp W13 publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2015.01.053 contributor: fullname: Zhu – volume: 7 start-page: 1 year: 2016 ident: 10.1016/j.ijbiomac.2019.08.020_bb0165 article-title: Characterization of a new cold-adapted and salt-activated polysaccharide lyase family 7 alginate lyase from Pseudoalteromonas sp. SM0524 publication-title: Front. Microbiol. doi: 10.3389/fmicb.2016.01120 contributor: fullname: Chen – year: 2006 ident: 10.1016/j.ijbiomac.2019.08.020_bb0005 contributor: fullname: Stephen – volume: 360 start-page: 69 year: 2012 ident: 10.1016/j.ijbiomac.2019.08.020_bb0080 article-title: cDNA cloning and bacterial expression of a PL-14 alginate lyase from a herbivorous marine snail Littorina brevicula publication-title: Carbohydr. Res. doi: 10.1016/j.carres.2012.05.019 contributor: fullname: Rahman – volume: 7 start-page: 1 issue: 1 year: 2017 ident: 10.1016/j.ijbiomac.2019.08.020_bb0065 article-title: Functional and structural studies of a multidomain alginate Lyase from Persicobacter sp. CCB-QB2 publication-title: Sci. Rep. doi: 10.1038/s41598-017-13288-1 contributor: fullname: Sim – volume: 37 start-page: 106 issue: 1 year: 2012 ident: 10.1016/j.ijbiomac.2019.08.020_bb0030 article-title: Alginate: properties and biomedical applications publication-title: Prog. Polym. Sci. doi: 10.1016/j.progpolymsci.2011.06.003 contributor: fullname: Lee – volume: 290 start-page: 505 issue: 2 year: 1999 ident: 10.1016/j.ijbiomac.2019.08.020_bb0240 article-title: Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 angstrom resolution publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1999.2883 contributor: fullname: Yoon – volume: 98 start-page: 1476 issue: 2 year: 2013 ident: 10.1016/j.ijbiomac.2019.08.020_bb0205 article-title: Purification and characterisation of a bifunctional alginate lyase from novel Isoptericola halotolerans CGMCC 5336 publication-title: Carbohydr. Polym. doi: 10.1016/j.carbpol.2013.07.050 contributor: fullname: Dou – volume: 67 start-page: 258 issue: 2 year: 2003 ident: 10.1016/j.ijbiomac.2019.08.020_bb0045 article-title: Enzymatically depolymerized alginate oligomers that cause cytotoxic cytokine production in human mononuclear cells publication-title: Biosci. Biotechnol. Biochem. doi: 10.1271/bbb.67.258 contributor: fullname: Iwamoto – volume: 110 start-page: 101 issue: 1 year: 1993 ident: 10.1016/j.ijbiomac.2019.08.020_bb0185 article-title: Sequence of a gene encoding a (poly mana) alginate lyase active on pseudomonas-aeruginosa alginate publication-title: FEMS Microbiol. Lett. doi: 10.1111/j.1574-6968.1993.tb06302.x contributor: fullname: Malissard – volume: 319 start-page: 575 issue: part 2 year: 1996 ident: 10.1016/j.ijbiomac.2019.08.020_bb0095 article-title: Cloning, sequencing and overexpression in Escherichia coli of the alginate lyase-encoding aly gene of pseudomonas alginovora: identification of three classes of alginate lyases publication-title: Biochem. J. doi: 10.1042/bj3190575 contributor: fullname: Chavagnat – volume: 108 start-page: 1140 year: 2018 ident: 10.1016/j.ijbiomac.2019.08.020_bb0255 article-title: Characterization of a new endo-type alginate lyase from Vibrio sp NJU-03 publication-title: Int. J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2017.10.164 contributor: fullname: Zhu – volume: 24 start-page: 295 issue: 2 year: 2012 ident: 10.1016/j.ijbiomac.2019.08.020_bb0050 article-title: Effect of molecular weight on the antioxidant property of low molecular weight alginate from Laminaria japonica publication-title: J. Appl. Phycol. doi: 10.1007/s10811-011-9679-y contributor: fullname: Zhao – volume: 34 start-page: 1087 issue: 6 year: 2012 ident: 10.1016/j.ijbiomac.2019.08.020_bb0265 article-title: Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans publication-title: Biotechnol. Lett. doi: 10.1007/s10529-012-0876-9 contributor: fullname: Kim – volume: 307 start-page: 9 issue: 1 year: 2001 ident: 10.1016/j.ijbiomac.2019.08.020_bb0285 article-title: Crystal structure of alginate lyase A1-III complexed with trisaccharide product at 2.0 angstrom resolution publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2000.4509 contributor: fullname: Yoon – volume: 1648 start-page: 62 issue: 1–2 year: 2003 ident: 10.1016/j.ijbiomac.2019.08.020_bb0245 article-title: Soluble human core 2 beta 6-N-acetylglucosaminyltransferase C2GnT1 requires its conserved cysteine residues for full activity publication-title: Biochim. Biophys Acta-Proteins Proteomics doi: 10.1016/S1570-9639(03)00105-5 contributor: fullname: Yang – volume: 19 start-page: 355 year: 2016 ident: 10.1016/j.ijbiomac.2019.08.020_bb0105 article-title: The alginate lyases FlAlyA, FlAlyB, FlAlyC, and FlAlex from Flavobacterium sp UMI-01 have distinct roles in the complete degradation of alginate publication-title: Algal Res. doi: 10.1016/j.algal.2016.03.008 contributor: fullname: Inoue – volume: 89 start-page: 199 issue: 2 year: 2000 ident: 10.1016/j.ijbiomac.2019.08.020_bb0190 article-title: Cloning and sequence analysis of a gene (aly PG) encoding poly(alpha-L-guluronate)lyase from Corynebacterium sp. strain ALY-1 publication-title: J. Biosci. Bioeng. doi: 10.1016/S1389-1723(00)88738-1 contributor: fullname: Matsubara – volume: 16 start-page: 1 issue: 9 year: 2018 ident: 10.1016/j.ijbiomac.2019.08.020_bb0230 article-title: Characterization of a novel PolyM-preferred alginate lyase from marine Vibrio splendidus OU02 publication-title: Mar. Drugs doi: 10.3390/md16090295 contributor: fullname: Zhuang – volume: 93 start-page: 1720 issue: 10 year: 2011 ident: 10.1016/j.ijbiomac.2019.08.020_bb0070 article-title: cDNA cloning of an alginate lyase from a marine gastropod Aplysia kurodai and assessment of catalytically important residues of this enzyme publication-title: Biochimie doi: 10.1016/j.biochi.2011.06.004 contributor: fullname: Rahman – volume: 8 start-page: 1 year: 2017 ident: 10.1016/j.ijbiomac.2019.08.020_bb0130 article-title: Alginate oligosaccharide DP5 exhibits antitumor effects in osteosarcoma patients following surgery publication-title: Front. Pharmacol. doi: 10.3389/fphar.2017.00623 contributor: fullname: Chen – volume: 64 start-page: 1067 issue: 5 year: 2000 ident: 10.1016/j.ijbiomac.2019.08.020_bb0040 article-title: Purification of alginate oligosaccharides with root growth-promoting activity toward lettuce publication-title: Biosci. Biotechnol. Biochem. doi: 10.1271/bbb.64.1067 contributor: fullname: Iwasaki – volume: 41 start-page: 828 issue: 6–7 year: 2007 ident: 10.1016/j.ijbiomac.2019.08.020_bb0215 article-title: Purification and characterization of a Na+/K+ dependent alginate lyase from turban shell gut Vibrio sp. YKW-34 publication-title: Enzym. Microb. Technol. doi: 10.1016/j.enzmictec.2007.07.003 contributor: fullname: Fu – volume: 182 start-page: 4572 issue: 16 year: 2000 ident: 10.1016/j.ijbiomac.2019.08.020_bb0195 article-title: Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate publication-title: J. Bacteriol. doi: 10.1128/JB.182.16.4572-4577.2000 contributor: fullname: Hashimoto – volume: 8 start-page: 481 issue: 5 year: 2006 ident: 10.1016/j.ijbiomac.2019.08.020_bb0180 article-title: Cloning and sequencing analysis of alginate lyase genes from the marine bacterium Vibrio sp. O2 publication-title: Mar. Biotechnol. doi: 10.1007/s10126-005-6157-z contributor: fullname: Kawamoto – volume: 13 start-page: 121 issue: 1 year: 2009 ident: 10.1016/j.ijbiomac.2019.08.020_bb0200 article-title: A new high-alkaline alginate lyase from a deep-sea bacterium Agarivorans sp publication-title: Extremophiles doi: 10.1007/s00792-008-0201-7 contributor: fullname: Kobayashi – volume: 54 start-page: 289 year: 2000 ident: 10.1016/j.ijbiomac.2019.08.020_bb0060 article-title: ALGINATE LYASE: review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications publication-title: Annu. Rev. Microbiol. doi: 10.1146/annurev.micro.54.1.289 contributor: fullname: Wong – volume: 42 start-page: 78 issue: 2 year: 2001 ident: 10.1016/j.ijbiomac.2019.08.020_bb0150 article-title: The release of alginate lyase from growing Pseudomonas syringae pathovar phaseolicola publication-title: Curr. Microbiol. doi: 10.1007/s002840010182 contributor: fullname: Ott – volume: 24 start-page: 545 issue: 4 year: 1992 ident: 10.1016/j.ijbiomac.2019.08.020_bb0010 article-title: Enzymic degradation of alginates publication-title: Int. J. Biochem. doi: 10.1016/0020-711X(92)90325-U contributor: fullname: Gacesa – volume: 352 start-page: 11 issue: 1 year: 2005 ident: 10.1016/j.ijbiomac.2019.08.020_bb0275 article-title: A structural basis for depolymerization of alginate by polysaccharide lyase family-7 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2005.06.075 contributor: fullname: Yamasaki – volume: 64 start-page: 519 issue: 4 year: 2017 ident: 10.1016/j.ijbiomac.2019.08.020_bb0115 article-title: Purification and characterization of a high salt-tolerant alginate lyase from Cobetia sp WG-007 publication-title: Biotechnol. Appl. Biochem. doi: 10.1002/bab.1506 contributor: fullname: Gong – volume: 338 start-page: 2841 issue: 24 year: 2003 ident: 10.1016/j.ijbiomac.2019.08.020_bb0075 article-title: cDNA cloning of an alginate lyase from abalone, Haliotis discus hannai publication-title: Carbohydr. Res. doi: 10.1016/j.carres.2003.08.009 contributor: fullname: Shimizu – volume: 40 start-page: 113 issue: 1 year: 2013 ident: 10.1016/j.ijbiomac.2019.08.020_bb0260 article-title: Characterization of a new alginate lyase from newly isolated Flavobacterium sp S20 publication-title: J. Ind. Microbiol. Biotechnol. doi: 10.1007/s10295-012-1210-1 contributor: fullname: Huang – volume: 58 start-page: 2474 issue: 8 year: 1992 ident: 10.1016/j.ijbiomac.2019.08.020_bb0220 article-title: Two types of bacterial alginate lyases publication-title: Appl. Environ. Microbiol. doi: 10.1128/AEM.58.8.2474-2478.1992 contributor: fullname: Kitamikado – volume: 12 start-page: 526 issue: 5 year: 2010 ident: 10.1016/j.ijbiomac.2019.08.020_bb0175 article-title: Cloning and sequencing of alginate lyase genes from deep-sea strains of Vibrio and Agarivorans and characterization of a new Vibrio enzyme publication-title: Mar. Biotechnol. doi: 10.1007/s10126-009-9237-7 contributor: fullname: Uchimura – volume: 54 start-page: 5.6.1 year: 2016 ident: 10.1016/j.ijbiomac.2019.08.020_bb0155 article-title: Comparative protein structure modeling using MODELLER publication-title: Curr. Protoc. Bioinformatics doi: 10.1002/cpbi.3 contributor: fullname: Webb – volume: 82 start-page: 239 year: 2018 ident: 10.1016/j.ijbiomac.2019.08.020_bb0025 article-title: Use of seaweed and filamentous fungus derived polysaccharides in the development of alginate-chitosan edible films containing fucoidan: study of moisture sorption, polyphenol release and antioxidant properties publication-title: Food Hydrocoll. doi: 10.1016/j.foodhyd.2018.03.056 contributor: fullname: Gomaa – volume: 9 start-page: 1 year: 2018 ident: 10.1016/j.ijbiomac.2019.08.020_bb0235 article-title: Expression and characterization of a new PolyG-specific alginate lyase from marine bacterium Microbulbifer sp Q7 publication-title: Front. Microbiol. doi: 10.3389/fmicb.2018.02894 contributor: fullname: Yang – volume: 350 start-page: 974 issue: 5 year: 2005 ident: 10.1016/j.ijbiomac.2019.08.020_bb0295 article-title: Crystal structure of Bacillus sp GL1 xanthan lyase complexed with a substrate: insights into the enzyme reaction mechanism publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2005.05.055 contributor: fullname: Maruyama – volume: 30 start-page: 2785 issue: 16 year: 2009 ident: 10.1016/j.ijbiomac.2019.08.020_bb0160 article-title: AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility publication-title: J. Comput. Chem. doi: 10.1002/jcc.21256 contributor: fullname: Morris – volume: 14 start-page: 2 issue: 6 year: 2016 ident: 10.1016/j.ijbiomac.2019.08.020_bb0110 article-title: Enzymatic hydrolysis of alginate to produce oligosaccharides by a new purified Endo-type alginate lyase publication-title: Mar. Drugs doi: 10.3390/md14060108 contributor: fullname: Zhu – volume: 21 start-page: 179 issue: 2 year: 2014 ident: 10.1016/j.ijbiomac.2019.08.020_bb0170 article-title: Structural and functional studies on three alginate lyases from Vibrio alginolyticus publication-title: Protein Pept Lett doi: 10.2174/09298665113206660094 contributor: fullname: Deng – volume: 35 start-page: 473 issue: 5 year: 2003 ident: 10.1016/j.ijbiomac.2019.08.020_bb0225 article-title: Purification and characterization of aginate lyase from marine bacterium Vibrio sp. QY101 publication-title: Acta Biochim. Biophys. Sin. contributor: fullname: Song – volume: 14 start-page: 189 issue: 2 year: 2012 ident: 10.1016/j.ijbiomac.2019.08.020_bb0210 article-title: Cloning and characterization of a novel oligoalginate lyase from a newly isolated bacterium Sphingomonas sp. MJ-3 publication-title: Mar. Biotechnol. doi: 10.1007/s10126-011-9402-7 contributor: fullname: Park – volume: 277 start-page: 119 issue: 1 year: 2000 ident: 10.1016/j.ijbiomac.2019.08.020_bb0125 article-title: Algal-lytic activities encoded by Chlorella virus CVK2 publication-title: Virology doi: 10.1006/viro.2000.0590 contributor: fullname: Sugimoto – volume: 55 start-page: 1850 issue: 5 year: 2018 ident: 10.1016/j.ijbiomac.2019.08.020_bb0135 article-title: Effects of alginate oligosaccharides with different molecular weights and guluronic to mannuronic acid ratios on glyceollin induction and accumulation in soybeans publication-title: J. Food Sci. Technol. doi: 10.1007/s13197-018-3101-6 contributor: fullname: Peng |
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| SubjectTerms | Alginate lyase Alginate oligosaccharides Alginates - metabolism Amino Acid Sequence Cloning, Molecular Computational Biology Hydrolysis Models, Molecular Polysaccharide-Lyases - chemistry Polysaccharide-Lyases - genetics Polysaccharide-Lyases - metabolism Protein Conformation Substrate Specificity Trisaccharide Trisaccharides - metabolism Vibrio - enzymology Vibrio - genetics |
| Title | Preparation of trisaccharides from alginate by a novel alginate lyase Alg7A from marine bacterium Vibrio sp. W13 |
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