Immobilization of Lecitase® Ultra onto the Organic Modified SBA-15 for Soybean Oil Degumming
In this study, SBA-15 was functionalized by organic groups (-CH3, -C4H9, -C8H17, -CH2CH2NH2, -C6H5, et al.), and then Lecitase® Ultra (LU) was immobilized onto the modified SBA-15 for soybean oil degumming. The hydrolysis activity, degumming performance, reusability in degumming, and the composition...
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| Published in | Journal of Oleo Science Vol. 71; no. 5; pp. 721 - 733 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English Japanese |
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Japan
Japan Oil Chemists' Society
01.01.2022
Japan Science and Technology Agency |
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| Abstract | In this study, SBA-15 was functionalized by organic groups (-CH3, -C4H9, -C8H17, -CH2CH2NH2, -C6H5, et al.), and then Lecitase® Ultra (LU) was immobilized onto the modified SBA-15 for soybean oil degumming. The hydrolysis activity, degumming performance, reusability in degumming, and the composition of phospholipids in the gum, of the immobilized LU samples, were carefully studied. Hydrolysis activities over 1800 U/g were obtained from all the immobilized LU samples. The highest activity of up to 4554.17 U/g was observed from the 3-ureidopropyl group-modified SBA-15-supported LU. Most of the immobilized LU samples removed the phospholipids effectively from crude soybean oil (initial phosphorous content 314.23 mg/kg), with a residual phosphorus content of less than 10 mg/kg. The reusability of the immobilized LU samples in the degumming process was evaluated. No loss of activity was observed from the methyl and N-(2-aminoethyl)-3-aminopropyl group-modified SBA-15-supported LU samples after five cycles of reuse. In addition, 3-aminopropyl and 3-glycidyloxypropyl group-modified SBA-15-supported LU samples retained over 90% of their initial activity; N-phenylaminomethyl and 1-isocyanatopropane group-functionalized SBA-15-supported LU samples retained approximately 80% of their initial activity. The phospholipids in the gum were analyzed. The n-octadecyl and N-(2-aminoethyl)-3-aminopropyl group-functionalized SBA-15-supported LU samples were selective for lysophosphatidylethanolamine (LPE) preparation, and LPE percentages up to 37.14 and 38.80% were obtained, respectively. The N-phenylaminomethyl group-modified SBA-15-supported LU showed selectivity toward lysophosphatidylcholine (LPC) production, with an LPC percentage of up to 38.5%. |
|---|---|
| AbstractList | In this study, SBA-15 was functionalized by organic groups (-CH
, -C
H
, -C
H
, -CH
CH
NH
, -C
H
, et al.), and then Lecitase
Ultra (LU) was immobilized onto the modified SBA-15 for soybean oil degumming. The hydrolysis activity, degumming performance, reusability in degumming, and the composition of phospholipids in the gum, of the immobilized LU samples, were carefully studied. Hydrolysis activities over 1800 U/g were obtained from all the immobilized LU samples. The highest activity of up to 4554.17 U/g was observed from the 3-ureidopropyl group-modified SBA-15-supported LU. Most of the immobilized LU samples removed the phospholipids effectively from crude soybean oil (initial phosphorous content 314.23 mg/kg), with a residual phosphorus content of less than 10 mg/kg. The reusability of the immobilized LU samples in the degumming process was evaluated. No loss of activity was observed from the methyl and N-(2-aminoethyl)-3-aminopropyl group-modified SBA-15-supported LU samples after five cycles of reuse. In addition, 3-aminopropyl and 3-glycidyloxypropyl group-modified SBA-15-supported LU samples retained over 90% of their initial activity; N-phenylaminomethyl and 1-isocyanatopropane group-functionalized SBA-15-supported LU samples retained approximately 80% of their initial activity. The phospholipids in the gum were analyzed. The n-octadecyl and N-(2-aminoethyl)-3-aminopropyl group-functionalized SBA-15-supported LU samples were selective for lysophosphatidylethanolamine (LPE) preparation, and LPE percentages up to 37.14 and 38.80% were obtained, respectively. The N-phenylaminomethyl group-modified SBA-15-supported LU showed selectivity toward lysophosphatidylcholine (LPC) production, with an LPC percentage of up to 38.5%. [Abstract :] In this study, SBA-15 was functionalized by organic groups (-CH3, -C4H9, -C8H17, -CH2CH2NH2, -C6H5, et al.), and then Lecitase(R) Ultra (LU) was immobilized onto the modified SBA-15 for soybean oil degumming. The hydrolysis activity, degumming performance, reusability in degumming, and the composition of phospholipids in the gum, of the immobilized LU samples, were carefully studied. Hydrolysis activities over 1800 U/g were obtained from all the immobilized LU samples. The highest activity of up to 4554.17 U/g was observed from the 3-ureidopropyl group-modified SBA-15-supported LU. Most of the immobilized LU samples removed the phospholipids effectively from crude soybean oil (initial phosphorous content 314.23 mg/kg), with a residual phosphorus content of less than 10 mg/kg. The reusability of the immobilized LU samples in the degumming process was evaluated. No loss of activity was observed from the methyl and N-(2-aminoethyl)-3-aminopropyl group-modified SBA-15-supported LU samples after five cycles of reuse. In addition, 3-aminopropyl and 3-glycidyloxypropyl group-modified SBA-15-supported LU samples retained over 90% of their initial activity ; N-phenylaminomethyl and 1-isocyanatopropane group-functionalized SBA-15-supported LU samples retained approximately 80% of their initial activity. The phospholipids in the gum were analyzed. The n-octadecyl and N-(2-aminoethyl)-3-aminopropyl group-functionalized SBA-15-supported LU samples were selective for lysophosphatidylethanolamine (LPE) preparation, and LPE percentages up to 37.14 and 38.80% were obtained, respectively. The N-phenylaminomethyl group-modified SBA-15-supported LU showed selectivity toward lysophosphatidylcholine (LPC) production, with an LPC percentage of up to 38.5%. In this study, SBA-15 was functionalized by organic groups (-CH3, -C4H9, -C8H17, -CH2CH2NH2, -C6H5, et al.), and then Lecitase® Ultra (LU) was immobilized onto the modified SBA-15 for soybean oil degumming. The hydrolysis activity, degumming performance, reusability in degumming, and the composition of phospholipids in the gum, of the immobilized LU samples, were carefully studied. Hydrolysis activities over 1800 U/g were obtained from all the immobilized LU samples. The highest activity of up to 4554.17 U/g was observed from the 3-ureidopropyl group-modified SBA-15-supported LU. Most of the immobilized LU samples removed the phospholipids effectively from crude soybean oil (initial phosphorous content 314.23 mg/kg), with a residual phosphorus content of less than 10 mg/kg. The reusability of the immobilized LU samples in the degumming process was evaluated. No loss of activity was observed from the methyl and N-(2-aminoethyl)-3-aminopropyl group-modified SBA-15-supported LU samples after five cycles of reuse. In addition, 3-aminopropyl and 3-glycidyloxypropyl group-modified SBA-15-supported LU samples retained over 90% of their initial activity; N-phenylaminomethyl and 1-isocyanatopropane group-functionalized SBA-15-supported LU samples retained approximately 80% of their initial activity. The phospholipids in the gum were analyzed. The n-octadecyl and N-(2-aminoethyl)-3-aminopropyl group-functionalized SBA-15-supported LU samples were selective for lysophosphatidylethanolamine (LPE) preparation, and LPE percentages up to 37.14 and 38.80% were obtained, respectively. The N-phenylaminomethyl group-modified SBA-15-supported LU showed selectivity toward lysophosphatidylcholine (LPC) production, with an LPC percentage of up to 38.5%. graphical abstract In this study, SBA-15 was functionalized by organic groups (-CH3, -C4H9, -C8H17, -CH2CH2NH2, -C6H5, et al.), and then Lecitase® Ultra (LU) was immobilized onto the modified SBA-15 for soybean oil degumming. The hydrolysis activity, degumming performance, reusability in degumming, and the composition of phospholipids in the gum, of the immobilized LU samples, were carefully studied. Hydrolysis activities over 1800 U/g were obtained from all the immobilized LU samples. The highest activity of up to 4554.17 U/g was observed from the 3-ureidopropyl group-modified SBA-15-supported LU. Most of the immobilized LU samples removed the phospholipids effectively from crude soybean oil (initial phosphorous content 314.23 mg/kg), with a residual phosphorus content of less than 10 mg/kg. The reusability of the immobilized LU samples in the degumming process was evaluated. No loss of activity was observed from the methyl and N-(2-aminoethyl)-3-aminopropyl group-modified SBA-15-supported LU samples after five cycles of reuse. In addition, 3-aminopropyl and 3-glycidyloxypropyl group-modified SBA-15-supported LU samples retained over 90% of their initial activity; N-phenylaminomethyl and 1-isocyanatopropane group-functionalized SBA-15-supported LU samples retained approximately 80% of their initial activity. The phospholipids in the gum were analyzed. The n-octadecyl and N-(2-aminoethyl)-3-aminopropyl group-functionalized SBA-15-supported LU samples were selective for lysophosphatidylethanolamine (LPE) preparation, and LPE percentages up to 37.14 and 38.80% were obtained, respectively. The N-phenylaminomethyl group-modified SBA-15-supported LU showed selectivity toward lysophosphatidylcholine (LPC) production, with an LPC percentage of up to 38.5%. |
| ArticleNumber | ess21353 |
| Author | Xu, Li Li, Lin Fan, Shudong Zhong, Nanjing Chen, Wenyi Li, Bing Huang, Jianrong Kou, Maomao |
| Author_xml | – sequence: 1 fullname: Chen, Wenyi organization: Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety – sequence: 2 fullname: Kou, Maomao organization: School of Food Science, Guangdong Pharmaceutical University – sequence: 3 fullname: Li, Lin organization: Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety – sequence: 4 fullname: Li, Bing organization: Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety – sequence: 5 fullname: Huang, Jianrong organization: School of Food Science, Guangdong Pharmaceutical University – sequence: 6 fullname: Fan, Shudong organization: Shandong Yuwang Ecological Food Co., Ltd – sequence: 7 fullname: Xu, Li organization: School of Chemistry and Chemical Engineering, Guangdong Pharmaceutical University – sequence: 8 fullname: Zhong, Nanjing organization: School of Food Science, Guangdong Pharmaceutical University |
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| CitedBy_id | crossref_primary_10_1016_j_foodchem_2022_135236 crossref_primary_10_1016_j_cofs_2023_100987 crossref_primary_10_1016_j_ijbiomac_2023_128804 crossref_primary_10_1007_s10098_023_02577_1 crossref_primary_10_1016_j_foodchem_2024_139624 |
| Cites_doi | 10.1016/j.lwt.2016.06.026 10.1007/s11746-008-1225-y 10.1007/s00253-019-09658-6 10.1016/j.mcat.2019.110405 10.1021/ie5045007 10.1007/s11746-008-1261-7 10.1016/j.biortech.2008.06.060 10.1007/s00217-013-2057-z 10.1002/jsfa.10140 10.1016/j.biortech.2011.05.050 10.1007/s00449-009-0316-y 10.1016/j.bbabio.2007.06.004 10.1016/j.procbio.2019.11.026 10.1002/ejlt.201000376 10.1016/j.procbio.2019.08.016 10.1002/jctb.2621 10.1002/mabi.201100127 10.1016/j.jfoodeng.2017.08.029 10.1016/j.lwt.2012.08.014 10.1016/j.procbio.2014.12.011 10.1007/s11746-011-1943-4 10.1016/B978-0-9888565-3-0.50009-1 10.1016/j.renene.2016.01.053 10.1016/j.molcatb.2008.07.008 10.1007/s11746-014-2555-6 10.5650/jos.ess19314 10.1016/j.biotechadv.2019.04.003 10.1039/b606481g 10.1016/j.molcata.2006.03.019 10.1016/j.ijbiomac.2018.08.155 10.1016/j.procbio.2018.09.019 10.1016/j.molcatb.2015.11.018 10.1016/j.jbiotec.2018.11.014 10.1016/j.foodchem.2018.07.185 10.3389/fbioe.2020.00036 10.1016/j.ijbiomac.2020.12.111 10.1016/j.cattod.2020.03.059 |
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| References | 14) Babaki, M.; Yousefi, M.; Habibi, Z.; Mohammadi, M.; Yousefi, P. et al. Enzymatic production of biodiesel using lipases immobilized on silica nanoparticles as highly reusable biocatalysts: Effect of water, t-butanol and blue silica gel contents. Renew. Energ. 91, 196-206 (2016). 3) Jiang, X.; Chang, M.; Jin, Q.; Wang, X. Application of phospholipase A1 and Phospholipase C in the degumming process of different kinds of crude oils. Process Biochem. 50, 432-437 (2015). 38) Yu, D.; Ma, Y.; Jiang, L.; Elfalleh, W.; Shi, M.; Hu, L. Optimization of magnetic immobilized phospholipase A1 degumming process for soybean oil using response surface methodology. Eur. Food Res. Technol. 237, 811-817 (2013). 39) Sheelu, G.; Kavitha, G.; Fadnavis, N.W. Efficient immobilization of Lecitase in gelatin hydrogel and degumming of rice bran oil using a spinning basket reactor. J. Am. Oil Chem. Soc. 85, 739-748 (2008). 5) Rossell, J.B.; Pritchard, J.L.R. Analysis of oilseeds, fats, and fatty foods in London. London: Elsevier Applied Science (1991). 17) Manjula, S.; Jose, A.; Divakar, S.; Subramanian, R. Degumming rice bran oil using phospholipase-A1. Eur. J. Lipid Sci. Tech. 113, 658-664 (2011). 13) Rodrigues, R.C.; Virgen-Ortíz, J.J.; dos Santos, J.C.S.; Berenguer-Murcia, Á.; Alcantara, A.R. et al. Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions. Biotechnol. Adv. 37, 746-770 (2019). 33) Li, Z.; Liu, H.; Zhao, G.; Wang, P.; Wang, L. et al. Enhancing the performance of a phospholipase A1 for oil degumming by bio-imprinting and immobilization. J. Mol. Catal. B-Enzym. 123, 122-131 (2016). 11) Silveira, E.A.; Moreno-Perez, S.; Basso, A.; Serban, S.; Pestana-Mamede, R. et al. Biocatalyst engineering of Thermomyces lanuginosus lipase adsorbed on hydrophobic supports: Modulation of enzyme properties for ethanolysis of oil in solvent-free systems. J. Biotechnol. 289, 126-134 (2019). 4) Yu, D.; Ma, Y.; Xue, S.J.; Jiang, L.; Shi, J. Characterization of immobilized phospolipase A1 on magnetic nanoparticles for oil degumming application. LWT-Food Sci. Technol. 50, 519-525 (2013). 31) Barth, A. Infrared spectroscopy of proteins. Biochim. Biophys. Acta 1767, 1073-1101 (2007). 32) Li, Y.; Zhong, N.; Cheong, L.Z.; Huang, J.; Chen, H.; Lin, S. Immobilization of Candida antarctica Lipase B onto organically-modified SBA-15 for efficient production of soybean-based mono and diacylglycerols. Int. J. Biol. Macromol. 120, 886-895 (2018). 18) Yang, B.; Zhou, R.; Yang, J.; Wang, Y.; Wang, W. Insight into the enzymatic degumming process of soybean oil. J. Am. Oil Chem. Soc. 85, 421-425 (2008). 28) GB/T 5537-2008 Inspection of grain and oils-Determination of phosphatide content. 1) More, N.S.; Gogate, P.R. Intensified degumming of crude soybean oil using cavitational reactors. J. Food Eng. 218, 33-43 (2018). 26) Miletić, N., Vuković, Z., Nastasović, A., Loos, K. Effect of Candida antarctica lipase B immobilization on the porous structure of the carrier. Macromol. Biosci. 11, 1537-1543 (2011). 2) Dayton, C.L.G.; Galhardo, F. Enzymatic degumming. in Green Vegetable Oil Processing (Farr, W.E.; Proctor, A. eds.), Academic press and AOCS press (2013). https://doi.org/10.1016/C2015-0-04080-1. 25) Kou, M.; Feng, S.; Zhong, N. Immobilization of Lecitase® Ultra onto the amino-functionalized SBA-15 and their applications in glycerolysis. J. Oleo Sci. 69, 347-358 (2020). 36) Wang, Y.; Zhao, M.; Ou, S.; Xie, L.; Tang, S. Preparation of a diacylglycerol-enriched soybean oil by phospholipase A1 catalyzed hydrolysis. J. Mol. Catal. B 56, 165-172 (2009). 16) Gao, S.; Wang, Y.; Wang, T.; Luo, G.; Dai, Y. Immobilization of lipase on methyl-modified silica aerogels by physical adsorption. Bioresour. Technol. 100, 996-999 (2009). 23) Zhong, N.; Chen, W.; Liu, L.; Chen, H. Immobilization of Rhizomucor miehei lipase onto the organic functionalized SBA-15: Their enzymatic properties and glycerolysis efficiencies for diacylglycerols production. Food Chem. 271, 739-746 (2019). 34) Boudrant, J.; Woodley, J.M.; Fernandez-Lafuente, R. Parameters necessary to define an immobilized enzyme preparation. Process Biochem. 90, 66-80 (2020). 7) Germinati, S.; Paoletti, L.; Aguirre, A.; Peirú, S.; Menzella, H.G.; Castelli, M.E. Industrial uses of phospholipases: Current state and future applications. Appl. Microbiol. Biot. 103, 2571-2582 (2019). 22) Zhao, X.; Zhao, F.; Zhong, N. Production of diacylglycerols through glycerolysis with SBA-15 supported Thermomyces lanuginosus lipase as catalyst. J. Sci. Food Agric. 100, 1426-1435 (2020). 27) Wang, X.; He, L.; Huang, J.; Zhong, N. Immobilization of lipases onto the halogen & haloalkanes modified SBA-15: Enzymatic activity and glycerolysis performance study. Int. J. Biol. Macromol. 169, 239-250 (2021). 8) Jiang, F.; Wang, J.; Kaleem, I.; Dai, D.; Zhou, X.; Li, C. Degumming of vegetable oils by a novel phospholipase B from Pseudomonas fluorescens BIT-18. Bioresour. Technol. 102, 8052-8056 (2011). 29) Xie, W.; Hu, L.; Yang, X. Basic ionic liquid supported on mesoporous SBA-15 silica as an efficient heterogeneous catalyst for biodiesel production. Ind. Eng. Chem. Res. 54, 1505-1512 (2015). 15) He, J.; Song, Z.; Ma, H.; Yang, L.; Guo, C. Formation of a mesoporous bioreactor based on SBA-15 and porcine pancreatic lipase by chemical modification following the uptake of enzymes. J. Mater. Chem. 16, 4307-4315 (2006). 30) Phan, N.T.; Jones, C.W. Highly accessible catalytic sites on recyclable organosilane-functionalized magnetic nanoparticles: An alternative to functionalized porous silica catalysts. J. Mol. Catal. A 253, 123-131 (2006). 12) Arana-Peña, S.; Rios, N.S.; Carballares, D.; Mendez-Sanchez, C.; Lokha, Y. et al. Effects of enzyme loading and immobilization conditions on the catalytic features of lipase from Pseudomonas fluorescens immobilized on octyl-agarose beads. Front. Bioeng. Biotech. 8, 1-13 (2020). 35) Pinheiro, M.P.; Monteiro, R.R.C.; Silva, F.F.M.; Lemos, T.L.G.; Fernandez-Lafuente, R. et al. Modulation of Lecitase properties via immobilization on differently activated Immobead-350: Stabilization and inversion of enantiospecificity. Process Biochem. 87, 128-137 (2019). 21) Virgen-Ortíz, J.J.; dos Santos, J.C.S.; Ortiz, C.; Berenguer-Murcia, Á.; Barbosa, O. et al. Lecitase ultra: A phospholipase with great potential in biocatalysis. Mol. Catal. 473, 110405 (2019). 19) Jiang, X.; Chang, M.; Wang, X.; Jin, Q.; Wang, X. A comparative study of phospholipase A1 and phospholipase C on soybean oil degumming. J. Am. Oil Chem. Soc. 91, 2125-2134 (2014). 37) Yu, D.; Wang, Y.; Yu, B.; Wang, T.; Zhang, R. et al. Numerical simulation and application of nanomagnetic enzyme in a liquid-solid magnetic fluidized bed. Process Biochem. 75, 121-129 (2018). 6) Jiang, F.; Wang, J.; Ju, L.; Kaleem, I.; Dai, D.; Li, C. Optimization of degumming process for soybean oil by phospholipase B. J. Chem. Technol. Biotechnol. 86, 1081-1087 (2011). 9) Qu, Y.; Sun, L.; Li, X.; Zhou, S.; Zhang, Q. et al. Enzymatic degumming of soybean oil with magnetic immobilized phospholipase A2. LWT-Food Sci. Technol. 73, 290-295 (2016). 10) Arana-Peña, S.; Rios, N,S.; Carballares, D.; Gonçalves, L.R.B.; Fernandez-Lafuente, R. Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions. Catal. Today 362, 130-140 (2021). 20) Yu, D.; Jiang, L.; Li, Z.; Shi, J.; Xue, J.; Kakuda, Y. Immobilization of phospholipase A1 and its application in soybean oil degumming. J. Am. Oil Chem. Soc. 89, 649-656 (2012). 24) Arica, M.Y.; Soydogan, H.; Bayramoglu, G. Reversible immobilization of Candida rugosa lipase on fibrous polymer grafted and sulfonated p (HEMA/EGDMA) beads. Bioproc. Biosyst. Eng. 33, 227-236 (2010). 22 23 24 25 26 27 28 29 30 31 10 32 11 33 12 34 13 35 14 36 15 37 16 38 17 39 18 19 1 2 3 4 5 6 7 8 9 20 21 |
| References_xml | – ident: 9 doi: 10.1016/j.lwt.2016.06.026 – ident: 18 doi: 10.1007/s11746-008-1225-y – ident: 7 doi: 10.1007/s00253-019-09658-6 – ident: 21 doi: 10.1016/j.mcat.2019.110405 – ident: 29 doi: 10.1021/ie5045007 – ident: 39 doi: 10.1007/s11746-008-1261-7 – ident: 16 doi: 10.1016/j.biortech.2008.06.060 – ident: 38 doi: 10.1007/s00217-013-2057-z – ident: 22 doi: 10.1002/jsfa.10140 – ident: 8 doi: 10.1016/j.biortech.2011.05.050 – ident: 24 doi: 10.1007/s00449-009-0316-y – ident: 31 doi: 10.1016/j.bbabio.2007.06.004 – ident: 34 doi: 10.1016/j.procbio.2019.11.026 – ident: 28 – ident: 17 doi: 10.1002/ejlt.201000376 – ident: 35 doi: 10.1016/j.procbio.2019.08.016 – ident: 6 doi: 10.1002/jctb.2621 – ident: 26 doi: 10.1002/mabi.201100127 – ident: 1 doi: 10.1016/j.jfoodeng.2017.08.029 – ident: 4 doi: 10.1016/j.lwt.2012.08.014 – ident: 3 doi: 10.1016/j.procbio.2014.12.011 – ident: 20 doi: 10.1007/s11746-011-1943-4 – ident: 2 doi: 10.1016/B978-0-9888565-3-0.50009-1 – ident: 14 doi: 10.1016/j.renene.2016.01.053 – ident: 36 doi: 10.1016/j.molcatb.2008.07.008 – ident: 5 – ident: 19 doi: 10.1007/s11746-014-2555-6 – ident: 25 doi: 10.5650/jos.ess19314 – ident: 13 doi: 10.1016/j.biotechadv.2019.04.003 – ident: 15 doi: 10.1039/b606481g – ident: 30 doi: 10.1016/j.molcata.2006.03.019 – ident: 32 doi: 10.1016/j.ijbiomac.2018.08.155 – ident: 37 doi: 10.1016/j.procbio.2018.09.019 – ident: 33 doi: 10.1016/j.molcatb.2015.11.018 – ident: 11 doi: 10.1016/j.jbiotec.2018.11.014 – ident: 23 doi: 10.1016/j.foodchem.2018.07.185 – ident: 12 doi: 10.3389/fbioe.2020.00036 – ident: 27 doi: 10.1016/j.ijbiomac.2020.12.111 – ident: 10 doi: 10.1016/j.cattod.2020.03.059 |
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| Snippet | In this study, SBA-15 was functionalized by organic groups (-CH3, -C4H9, -C8H17, -CH2CH2NH2, -C6H5, et al.), and then Lecitase® Ultra (LU) was immobilized onto... [Abstract :] In this study, SBA-15 was functionalized by organic groups (-CH3, -C4H9, -C8H17, -CH2CH2NH2, -C6H5, et al.), and then Lecitase(R) Ultra (LU) was... In this study, SBA-15 was functionalized by organic groups (-CH , -C H , -C H , -CH CH NH , -C H , et al.), and then Lecitase Ultra (LU) was immobilized onto... |
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| SubjectTerms | Degumming enzyme degumming Enzymes, Immobilized Hydrolysis Lecitase® Ultra organic modification Phospholipids SBA-15 Selectivity Silicon Dioxide Soybean Oil Soybeans Vegetable oils |
| Title | Immobilization of Lecitase® Ultra onto the Organic Modified SBA-15 for Soybean Oil Degumming |
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