Mutagenesis and characterization of a Bacillus amyloliquefaciens strain for Cinnamomum camphora seed kernel oil extraction by aqueous enzymatic method

The purpose of the present study was to increase the proteinase activity of the strain NCU116 by combining ultraviolet irradiation and N -methyl- N′ -nitro- N -nitroso guanidine treatment, in order to enhance the efficiency of Cinnamomum camphora seed kernel oil (CCSKO) extraction by aqueous enzymat...

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Published inAMB Express Vol. 7; no. 1; pp. 154 - 10
Main Authors Zeng, Cheng, Zhao, Rongbin, Ma, Maomao, Zeng, Zheling, Gong, Deming
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Springer Berlin Heidelberg 17.07.2017
Springer Nature B.V
SpringerOpen
Subjects
Amylases
Aqueous enzymatic method
Bacillus amyloliquefacien
Biomedical and Life Sciences
Biotechnology
Calcium
Cellulase
Copper
Enzymatic properties
Enzymes
Extracellular enzymes
Extraction
Glucoamylase
Guanidine
Iron
Irradiation
Life Sciences
Microbial Genetics and Genomics
Microbiology
Milk
Mutagenesis
Oils & fats
Original
Original Article
Pectinase
Proteinase
Skim milk
Temperature effects
Ultraviolet radiation
UV and NTG mutation
UV and NTG mutation
Aqueous enzymatic method
Proteinase
Enzymatic properties
Bacillus amyloliquefacien
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Abstract The purpose of the present study was to increase the proteinase activity of the strain NCU116 by combining ultraviolet irradiation and N -methyl- N′ -nitro- N -nitroso guanidine treatment, in order to enhance the efficiency of Cinnamomum camphora seed kernel oil (CCSKO) extraction by aqueous enzymatic method (AEM). The mutated strain, designated as NCU116-1, was screened out by the ratio of hydrolytic zone diameter to colony diameter on skim milk plate. The proteinase activity (9116.1 U/ml) of NCU116-1 was increased by 31.9% compared with the parental strain. The extracellular enzymes produced by NCU116-1 included proteinase, pectase, glucoamylase, cellulase and amylase. The proteinase had the maximum activity at 50 °C. Its optimum temperature and pH value were approximately 45 °C and 8.0 respectively. Mn 2+ was an activator of neutral proteinase. The glucoamylase had the maximum activity at 35 °C, and was activated by Cu 2+ , Fe 3+ and Mn 2+ . Its optimum temperatures and pH value were 35 °C and 8.0 respectively. The pectinase had the maximum activity at 40 °C, and was activated by Ca 2+ and Mn 2+ . Its optimum temperatures and pH value were 35–40 °C and 6.0 respectively. The optimum conditions of CCSKO extraction by AEM were also investigated. The results suggested that the best amount of enzyme solution and enzymolysis time were 20% (v/v) and 4 h, respectively. The oil extraction rate was 95.2% under these conditions. Thus, a suitable mutated strain was selected for CCSKO extraction by AEM and the optimum extraction conditions were determined.
AbstractList The purpose of the present study was to increase the proteinase activity of the strain NCU116 by combining ultraviolet irradiation and N -methyl- N′ -nitro- N -nitroso guanidine treatment, in order to enhance the efficiency of Cinnamomum camphora seed kernel oil (CCSKO) extraction by aqueous enzymatic method (AEM). The mutated strain, designated as NCU116-1, was screened out by the ratio of hydrolytic zone diameter to colony diameter on skim milk plate. The proteinase activity (9116.1 U/ml) of NCU116-1 was increased by 31.9% compared with the parental strain. The extracellular enzymes produced by NCU116-1 included proteinase, pectase, glucoamylase, cellulase and amylase. The proteinase had the maximum activity at 50 °C. Its optimum temperature and pH value were approximately 45 °C and 8.0 respectively. Mn 2+ was an activator of neutral proteinase. The glucoamylase had the maximum activity at 35 °C, and was activated by Cu 2+ , Fe 3+ and Mn 2+ . Its optimum temperatures and pH value were 35 °C and 8.0 respectively. The pectinase had the maximum activity at 40 °C, and was activated by Ca 2+ and Mn 2+ . Its optimum temperatures and pH value were 35–40 °C and 6.0 respectively. The optimum conditions of CCSKO extraction by AEM were also investigated. The results suggested that the best amount of enzyme solution and enzymolysis time were 20% (v/v) and 4 h, respectively. The oil extraction rate was 95.2% under these conditions. Thus, a suitable mutated strain was selected for CCSKO extraction by AEM and the optimum extraction conditions were determined.
Abstract The purpose of the present study was to increase the proteinase activity of the strain NCU116 by combining ultraviolet irradiation and N-methyl-N′-nitro-N-nitroso guanidine treatment, in order to enhance the efficiency of Cinnamomum camphora seed kernel oil (CCSKO) extraction by aqueous enzymatic method (AEM). The mutated strain, designated as NCU116-1, was screened out by the ratio of hydrolytic zone diameter to colony diameter on skim milk plate. The proteinase activity (9116.1 U/ml) of NCU116-1 was increased by 31.9% compared with the parental strain. The extracellular enzymes produced by NCU116-1 included proteinase, pectase, glucoamylase, cellulase and amylase. The proteinase had the maximum activity at 50 °C. Its optimum temperature and pH value were approximately 45 °C and 8.0 respectively. Mn2+ was an activator of neutral proteinase. The glucoamylase had the maximum activity at 35 °C, and was activated by Cu2+, Fe3+ and Mn2+. Its optimum temperatures and pH value were 35 °C and 8.0 respectively. The pectinase had the maximum activity at 40 °C, and was activated by Ca2+ and Mn2+. Its optimum temperatures and pH value were 35–40 °C and 6.0 respectively. The optimum conditions of CCSKO extraction by AEM were also investigated. The results suggested that the best amount of enzyme solution and enzymolysis time were 20% (v/v) and 4 h, respectively. The oil extraction rate was 95.2% under these conditions. Thus, a suitable mutated strain was selected for CCSKO extraction by AEM and the optimum extraction conditions were determined.
The purpose of the present study was to increase the proteinase activity of the strain NCU116 by combining ultraviolet irradiation and N-methyl-N'-nitro-N-nitroso guanidine treatment, in order to enhance the efficiency of Cinnamomum camphora seed kernel oil (CCSKO) extraction by aqueous enzymatic method (AEM). The mutated strain, designated as NCU116-1, was screened out by the ratio of hydrolytic zone diameter to colony diameter on skim milk plate. The proteinase activity (9116.1 U/ml) of NCU116-1 was increased by 31.9% compared with the parental strain. The extracellular enzymes produced by NCU116-1 included proteinase, pectase, glucoamylase, cellulase and amylase. The proteinase had the maximum activity at 50 °C. Its optimum temperature and pH value were approximately 45 °C and 8.0 respectively. Mn2+ was an activator of neutral proteinase. The glucoamylase had the maximum activity at 35 °C, and was activated by Cu2+, Fe3+ and Mn2+. Its optimum temperatures and pH value were 35 °C and 8.0 respectively. The pectinase had the maximum activity at 40 °C, and was activated by Ca2+ and Mn2+. Its optimum temperatures and pH value were 35-40 °C and 6.0 respectively. The optimum conditions of CCSKO extraction by AEM were also investigated. The results suggested that the best amount of enzyme solution and enzymolysis time were 20% (v/v) and 4 h, respectively. The oil extraction rate was 95.2% under these conditions. Thus, a suitable mutated strain was selected for CCSKO extraction by AEM and the optimum extraction conditions were determined.
The purpose of the present study was to increase the proteinase activity of the strain NCU116 by combining ultraviolet irradiation and N-methyl-N'-nitro-N-nitroso guanidine treatment, in order to enhance the efficiency of Cinnamomum camphora seed kernel oil (CCSKO) extraction by aqueous enzymatic method (AEM). The mutated strain, designated as NCU116-1, was screened out by the ratio of hydrolytic zone diameter to colony diameter on skim milk plate. The proteinase activity (9116.1 U/ml) of NCU116-1 was increased by 31.9% compared with the parental strain. The extracellular enzymes produced by NCU116-1 included proteinase, pectase, glucoamylase, cellulase and amylase. The proteinase had the maximum activity at 50 °C. Its optimum temperature and pH value were approximately 45 °C and 8.0 respectively. Mn was an activator of neutral proteinase. The glucoamylase had the maximum activity at 35 °C, and was activated by Cu , Fe and Mn . Its optimum temperatures and pH value were 35 °C and 8.0 respectively. The pectinase had the maximum activity at 40 °C, and was activated by Ca and Mn . Its optimum temperatures and pH value were 35-40 °C and 6.0 respectively. The optimum conditions of CCSKO extraction by AEM were also investigated. The results suggested that the best amount of enzyme solution and enzymolysis time were 20% (v/v) and 4 h, respectively. The oil extraction rate was 95.2% under these conditions. Thus, a suitable mutated strain was selected for CCSKO extraction by AEM and the optimum extraction conditions were determined.
ArticleNumber 154
Author Ma, Maomao
Zhao, Rongbin
Zeng, Cheng
Zeng, Zheling
Gong, Deming
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  surname: Zhao
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  givenname: Zheling
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  email: dgong01@gmail.com
  organization: State Key Laboratory of Food Science and Technology, Nanchang University, Jiangxi Province Key Laboratory of Edible and Medicinal Plant Resources, Nanchang University, New Zealand Institute of Natural Medicine Research
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Cites_doi 10.1007/s12010-009-8865-8
10.1016/j.enzmictec.2010.10.003
10.1016/j.biochi.2010.01.008
10.1016/j.molcatb.2014.01.002
10.3109/09637486.2016.1153611
10.1023/A:1023988110064
10.1111/j.1750-3841.2009.01300.x
10.1016/S0141-0229(00)00351-3
10.1016/j.foodhyd.2006.10.009
10.1016/j.jand.2014.10.022
10.1016/j.jtusci.2014.04.010
10.2337/db08-1557
10.1007/s12257-010-0410-7
10.1016/j.jbiotec.2006.02.021
10.1111/1750-3841.12943
10.1111/jpn.12030
10.1016/j.micres.2009.04.001
10.1016/j.tibtech.2011.06.014
10.1016/j.foodcont.2017.02.031
10.1016/j.jfoodeng.2013.01.014
10.1007/s13213-013-0685-y
10.1016/j.ejbt.2015.04.001
10.1111/j.1472-765X.2006.02039.x
10.1016/j.foodcont.2014.06.017
10.1016/j.tifs.2014.09.003
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Issue 1
Keywords UV and NTG mutation
Aqueous enzymatic method
Proteinase
Enzymatic properties
Bacillus amyloliquefacien
Language English
License Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
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References Yusoff, Gordon, Niranjan (CR28) 2015; 41
Hui, Wei, Cui, Zhao, Feng (CR12) 2009; 74
Babu, Sajina, Minoo, John, Mini, Tushar, Rema, Ravindran (CR3) 2003; 74
Pant, Prakash, Pavani, Bera, Deviram, Kumar, Panchpuri, Prasuna (CR21) 2015; 9
Wang, Liu, Liu, Cheng, Ma, Huang, Zhang (CR26) 2007; 44
Fu, Wang, Gong, Zeng, Jiang, Zeng (CR6) 2015; 80
Jaouadi, Aghajari, Haser, Bejar (CR14) 2010; 92
Azmir, Zaidul, Rahman, Sharif, Mohamed, Sahena, Jahurulb, Ghafoorc, Norulainid, Omar (CR2) 2013; 117
Funami, Zhang, Hiroe, Noda, Nakauma, Asai, Cowman, Al-Assaf, Phillips (CR7) 2007; 21
Lian, Huang, Ren, Ji, Zhu, Jin (CR17) 2010; 162
Ferreira, Lisenko, Barros, Zangeronimo, Pereira, Sousa (CR5) 2013; 98
Ibrahim, Al-Salamah, Elbadawi, El-Tayeb, Ibrahim (CR13) 2015; 18
Berlin, Balakshin, Gilkes, Kadla, Maximenko, Kubo, Saddler (CR4) 2006; 125
Li, Yang, Roy, Park, Jiang, Wang, Miao (CR16) 2010; 165
Puri, Sharma, Barrow (CR22) 2012; 30
CR8
Afifi, Abo-Elmagd, Housseiny (CR1) 2014; 64
Mumme, Stonehouse (CR19) 2015; 115
CR9
Rosenthal, Pyle, Niranjan, Gilmour, Trinca (CR24) 2001; 28
Hernandez, Fernandezlafuente (CR11) 2011; 48
CR23
CR01
Wang, Fu, Li, Gong, Wen, Yu, Zeng (CR27) 2016; 67
Luo, Zeng, Gong, Zhao, Liang, Zeng (CR18) 2014; 46
Page, Williamson, Yu, McNay, Dzuira, McCrimmon, Sherwin (CR20) 2009; 58
Zeng, Zhao, Wen, Yu, Zeng, Deng, Gong (CR29) 2017; 78
Subhedar, Gogate (CR25) 2014; 101
Haddar, Hmidet, Ghorbel-Bellaaj, Fakhfakh-Zouari, Sellami-Kamoun, Nasri (CR10) 2011; 16
16621087 - J Biotechnol. 2006 Sep 1;125(2):198-209
23298149 - J Anim Physiol Anim Nutr (Berl). 2014 Feb;98(1):1-8
19967469 - Appl Biochem Biotechnol. 2010 Oct;162(4):935-41
21816495 - Trends Biotechnol. 2012 Jan;30(1):37-44
11267644 - Enzyme Microb Technol. 2001 Apr 5;28(6):499-509
17209806 - Lett Appl Microbiol. 2007 Jan;44(1):1-6
19656667 - Microbiol Res. 2010 Mar 31;165(3):190-8
26130050 - J Food Sci. 2015 Aug;80(8):H1912-7
20096326 - Biochimie. 2010 Apr;92(4):360-9
19223595 - Diabetes. 2009 May;58(5):1237-44
26932533 - Int J Food Sci Nutr. 2016;67(3):288-97
25636220 - J Acad Nutr Diet. 2015 Feb;115(2):249-63
19895490 - J Food Sci. 2009 Sep;74(7):M418-21
22112819 - Enzyme Microb Technol. 2011 Feb 8;48(2):107-22
PB Subhedar (451_CR25) 2014; 101
M Lian (451_CR17) 2010; 162
M Puri (451_CR22) 2012; 30
K Mumme (451_CR19) 2015; 115
J Azmir (451_CR2) 2013; 117
KN Babu (451_CR3) 2003; 74
C Zeng (451_CR29) 2017; 78
AS Ibrahim (451_CR13) 2015; 18
H Wang (451_CR26) 2007; 44
KA Page (451_CR20) 2009; 58
G Pant (451_CR21) 2015; 9
T Funami (451_CR7) 2007; 21
B Jaouadi (451_CR14) 2010; 92
A Haddar (451_CR10) 2011; 16
451_CR23
451_CR01
C Luo (451_CR18) 2014; 46
AF Afifi (451_CR1) 2014; 64
451_CR9
B Wang (451_CR27) 2016; 67
451_CR8
X Li (451_CR16) 2010; 165
MM Yusoff (451_CR28) 2015; 41
L Ferreira (451_CR5) 2013; 98
Z Hui (451_CR12) 2009; 74
J Fu (451_CR6) 2015; 80
K Hernandez (451_CR11) 2011; 48
A Berlin (451_CR4) 2006; 125
A Rosenthal (451_CR24) 2001; 28
References_xml – volume: 162
  start-page: 935
  year: 2010
  end-page: 941
  ident: CR17
  article-title: Increase of docosahexaenoic acid production by sp. through mutagenesis and enzyme assay
  publication-title: Appl Biochem Biotechnol
  doi: 10.1007/s12010-009-8865-8
  contributor:
    fullname: Jin
– volume: 48
  start-page: 107
  year: 2011
  end-page: 122
  ident: CR11
  article-title: Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance
  publication-title: Enzyme Microb Technol
  doi: 10.1016/j.enzmictec.2010.10.003
  contributor:
    fullname: Fernandezlafuente
– volume: 92
  start-page: 360
  year: 2010
  end-page: 369
  ident: CR14
  article-title: Enhancement of the thermostability and the catalytic efficiency of CBS protease by site-directed mutagenesis
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2010.01.008
  contributor:
    fullname: Bejar
– volume: 101
  start-page: 108
  year: 2014
  end-page: 114
  ident: CR25
  article-title: Enhancing the activity of cellulase enzyme using ultrasonic irradiations
  publication-title: J Mol Catal B Enzym
  doi: 10.1016/j.molcatb.2014.01.002
  contributor:
    fullname: Gogate
– volume: 67
  start-page: 288
  year: 2016
  end-page: 297
  ident: CR27
  article-title: Medium-chain fatty acid reduces lipid accumulation by regulating expression of lipid-sensing genes in human liver cells with steatosis
  publication-title: Int J Food Sci Nutr
  doi: 10.3109/09637486.2016.1153611
  contributor:
    fullname: Zeng
– volume: 74
  start-page: 179
  year: 2003
  end-page: 183
  ident: CR3
  article-title: Micropropagation of camphor tree ( )
  publication-title: Plant Cell Tissue Organ
  doi: 10.1023/A:1023988110064
  contributor:
    fullname: Ravindran
– volume: 74
  start-page: M418
  year: 2009
  end-page: M421
  ident: CR12
  article-title: Antibacterial interactions of monolaurin with commonly used antimicrobials and food components
  publication-title: J Food Sci
  doi: 10.1111/j.1750-3841.2009.01300.x
  contributor:
    fullname: Feng
– ident: CR8
– volume: 28
  start-page: 499
  year: 2001
  end-page: 509
  ident: CR24
  article-title: Combined effect of operational variables and enzyme activity on aqueous enzymatic extraction of oil and protein from soybean
  publication-title: Enzyme Microb Technol
  doi: 10.1016/S0141-0229(00)00351-3
  contributor:
    fullname: Trinca
– volume: 21
  start-page: 1319
  year: 2007
  end-page: 1329
  ident: CR7
  article-title: Effects of the proteinaceous moiety on the emulsifying properties of sugar beet pectin
  publication-title: Food Hydrocoll
  doi: 10.1016/j.foodhyd.2006.10.009
  contributor:
    fullname: Phillips
– volume: 115
  start-page: 249
  year: 2015
  end-page: 263
  ident: CR19
  article-title: Effects of medium-chain triglycerides on weight loss and body composition: a meta-analysis of randomized controlled trials
  publication-title: J Acad Nutr Diet
  doi: 10.1016/j.jand.2014.10.022
  contributor:
    fullname: Stonehouse
– volume: 9
  start-page: 50
  year: 2015
  end-page: 55
  ident: CR21
  article-title: Production, optimization and partial purification of protease from
  publication-title: J Taibah Univ Sci
  doi: 10.1016/j.jtusci.2014.04.010
  contributor:
    fullname: Prasuna
– volume: 58
  start-page: 1237
  year: 2009
  end-page: 1244
  ident: CR20
  article-title: Medium-chain fatty acids improve cognitive function in intensively treated type 1 diabetic patients and support in vitro synaptic transmission during acute hypoglycemia
  publication-title: Diabetes
  doi: 10.2337/db08-1557
  contributor:
    fullname: Sherwin
– ident: CR23
– volume: 16
  start-page: 669
  year: 2011
  end-page: 678
  ident: CR10
  article-title: Alkaline proteases produced by RP1 grown on shrimp wastes: application in chitin extraction, chicken feather-degradation and as a dehairing agent
  publication-title: Biotechnol Bioprocess Eng
  doi: 10.1007/s12257-010-0410-7
  contributor:
    fullname: Nasri
– volume: 125
  start-page: 198
  year: 2006
  end-page: 209
  ident: CR4
  article-title: Inhibition of cellulase, xylanase and β-glucosidase activities by softwood lignin preparations
  publication-title: J Biotechnol
  doi: 10.1016/j.jbiotec.2006.02.021
  contributor:
    fullname: Saddler
– volume: 80
  start-page: H1912
  year: 2015
  end-page: H1917
  ident: CR6
  article-title: Camphor tree seed kernel oil reduces body fat deposition and improves blood lipids in rats
  publication-title: J Food Sci
  doi: 10.1111/1750-3841.12943
  contributor:
    fullname: Zeng
– volume: 98
  start-page: 1
  year: 2013
  end-page: 8
  ident: CR5
  article-title: Influence of medium-chain triglycerides on consumption and weight gain in rats: a systematic review
  publication-title: J Anim Physiol Anim Nutr
  doi: 10.1111/jpn.12030
  contributor:
    fullname: Sousa
– volume: 165
  start-page: 190
  year: 2010
  end-page: 198
  ident: CR16
  article-title: Enhanced cellulase production of the mutated by microwave and ultraviolet
  publication-title: Microbiol Res
  doi: 10.1016/j.micres.2009.04.001
  contributor:
    fullname: Miao
– volume: 30
  start-page: 37
  year: 2012
  end-page: 44
  ident: CR22
  article-title: Enzyme-assisted extraction of bioactives from plants
  publication-title: Trends Biotechnol
  doi: 10.1016/j.tibtech.2011.06.014
  contributor:
    fullname: Barrow
– volume: 78
  start-page: 24
  year: 2017
  end-page: 32
  ident: CR29
  article-title: Screening and identification of a strain for aqueous enzymatic extraction of medium-chain triglycerides
  publication-title: Food Control
  doi: 10.1016/j.foodcont.2017.02.031
  contributor:
    fullname: Gong
– volume: 117
  start-page: 426
  year: 2013
  end-page: 436
  ident: CR2
  article-title: Techniques for extraction of bioactive compounds from plant materials: a review
  publication-title: J Food Eng
  doi: 10.1016/j.jfoodeng.2013.01.014
  contributor:
    fullname: Omar
– ident: CR9
– volume: 64
  start-page: 521
  year: 2014
  end-page: 530
  ident: CR1
  article-title: Improvement of alkaline protease production by NRRL 792 through physical and chemical mutation, optimization, characterization and genetic variation between mutant and wild-type strains
  publication-title: Ann Microbiol
  doi: 10.1007/s13213-013-0685-y
  contributor:
    fullname: Housseiny
– volume: 18
  start-page: 236
  year: 2015
  end-page: 243
  ident: CR13
  article-title: Production of extracellular alkaline protease by new halotolerant alkaliphilic sp. NPST-AK15 isolated from hyper saline soda lakes
  publication-title: Electron J Biotechnol
  doi: 10.1016/j.ejbt.2015.04.001
  contributor:
    fullname: Ibrahim
– volume: 44
  start-page: 1
  year: 2007
  end-page: 6
  ident: CR26
  article-title: Screening and mutagenesis of a novel strain producing alkaline protease for dehairing
  publication-title: Lett Appl Microbiol
  doi: 10.1111/j.1472-765X.2006.02039.x
  contributor:
    fullname: Zhang
– volume: 46
  start-page: 488
  year: 2014
  end-page: 494
  ident: CR18
  article-title: Evaluation of monolaurin from camphor tree seeds for controlling food spoilage fungi
  publication-title: Food Control
  doi: 10.1016/j.foodcont.2014.06.017
  contributor:
    fullname: Zeng
– volume: 41
  start-page: 60
  year: 2015
  end-page: 82
  ident: CR28
  article-title: Aqueous enzyme assisted oil extraction from oilseeds and emulsion de-emulsifying methods: a review
  publication-title: Trends Food Sci Technol
  doi: 10.1016/j.tifs.2014.09.003
  contributor:
    fullname: Niranjan
– ident: CR01
– volume: 30
  start-page: 37
  year: 2012
  ident: 451_CR22
  publication-title: Trends Biotechnol
  doi: 10.1016/j.tibtech.2011.06.014
  contributor:
    fullname: M Puri
– volume: 80
  start-page: H1912
  year: 2015
  ident: 451_CR6
  publication-title: J Food Sci
  doi: 10.1016/j.foodhyd.2006.10.009
  contributor:
    fullname: J Fu
– volume: 74
  start-page: M418
  year: 2009
  ident: 451_CR12
  publication-title: J Food Sci
  doi: 10.1111/j.1750-3841.2009.01300.x
  contributor:
    fullname: Z Hui
– volume: 46
  start-page: 488
  year: 2014
  ident: 451_CR18
  publication-title: Food Control
  doi: 10.1016/j.foodcont.2014.06.017
  contributor:
    fullname: C Luo
– ident: 451_CR01
– volume: 18
  start-page: 236
  year: 2015
  ident: 451_CR13
  publication-title: Electron J Biotechnol
  doi: 10.1016/j.ejbt.2015.04.001
  contributor:
    fullname: AS Ibrahim
– ident: 451_CR8
– volume: 9
  start-page: 50
  year: 2015
  ident: 451_CR21
  publication-title: J Taibah Univ Sci
  doi: 10.1016/j.jtusci.2014.04.010
  contributor:
    fullname: G Pant
– volume: 125
  start-page: 198
  year: 2006
  ident: 451_CR4
  publication-title: J Biotechnol
  doi: 10.1016/j.jbiotec.2006.02.021
  contributor:
    fullname: A Berlin
– volume: 165
  start-page: 190
  year: 2010
  ident: 451_CR16
  publication-title: Microbiol Res
  doi: 10.1016/j.micres.2009.04.001
  contributor:
    fullname: X Li
– volume: 16
  start-page: 669
  year: 2011
  ident: 451_CR10
  publication-title: Biotechnol Bioprocess Eng
  doi: 10.1007/s12257-010-0410-7
  contributor:
    fullname: A Haddar
– volume: 44
  start-page: 1
  year: 2007
  ident: 451_CR26
  publication-title: Lett Appl Microbiol
  doi: 10.1111/j.1472-765X.2006.02039.x
  contributor:
    fullname: H Wang
– ident: 451_CR9
– ident: 451_CR23
– volume: 101
  start-page: 108
  year: 2014
  ident: 451_CR25
  publication-title: J Mol Catal B Enzym
  doi: 10.1016/j.molcatb.2014.01.002
  contributor:
    fullname: PB Subhedar
– volume: 98
  start-page: 1
  year: 2013
  ident: 451_CR5
  publication-title: J Anim Physiol Anim Nutr
  doi: 10.1111/jpn.12030
  contributor:
    fullname: L Ferreira
– volume: 21
  start-page: 1319
  year: 2007
  ident: 451_CR7
  publication-title: Food Hydrocoll
  doi: 10.1016/j.foodhyd.2006.10.009
  contributor:
    fullname: T Funami
– volume: 92
  start-page: 360
  year: 2010
  ident: 451_CR14
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2010.01.008
  contributor:
    fullname: B Jaouadi
– volume: 28
  start-page: 499
  year: 2001
  ident: 451_CR24
  publication-title: Enzyme Microb Technol
  doi: 10.1016/S0141-0229(00)00351-3
  contributor:
    fullname: A Rosenthal
– volume: 78
  start-page: 24
  year: 2017
  ident: 451_CR29
  publication-title: Food Control
  doi: 10.1016/j.foodcont.2017.02.031
  contributor:
    fullname: C Zeng
– volume: 115
  start-page: 249
  year: 2015
  ident: 451_CR19
  publication-title: J Acad Nutr Diet
  doi: 10.1016/j.jand.2014.10.022
  contributor:
    fullname: K Mumme
– volume: 117
  start-page: 426
  year: 2013
  ident: 451_CR2
  publication-title: J Food Eng
  doi: 10.1016/j.jfoodeng.2013.01.014
  contributor:
    fullname: J Azmir
– volume: 48
  start-page: 107
  year: 2011
  ident: 451_CR11
  publication-title: Enzyme Microb Technol
  doi: 10.1016/j.enzmictec.2010.10.003
  contributor:
    fullname: K Hernandez
– volume: 74
  start-page: 179
  year: 2003
  ident: 451_CR3
  publication-title: Plant Cell Tissue Organ
  doi: 10.1023/A:1023988110064
  contributor:
    fullname: KN Babu
– volume: 58
  start-page: 1237
  year: 2009
  ident: 451_CR20
  publication-title: Diabetes
  doi: 10.2337/db08-1557
  contributor:
    fullname: KA Page
– volume: 67
  start-page: 288
  year: 2016
  ident: 451_CR27
  publication-title: Int J Food Sci Nutr
  doi: 10.3109/09637486.2016.1153611
  contributor:
    fullname: B Wang
– volume: 64
  start-page: 521
  year: 2014
  ident: 451_CR1
  publication-title: Ann Microbiol
  doi: 10.1007/s13213-013-0685-y
  contributor:
    fullname: AF Afifi
– volume: 162
  start-page: 935
  year: 2010
  ident: 451_CR17
  publication-title: Appl Biochem Biotechnol
  doi: 10.1007/s12010-009-8865-8
  contributor:
    fullname: M Lian
– volume: 41
  start-page: 60
  year: 2015
  ident: 451_CR28
  publication-title: Trends Food Sci Technol
  doi: 10.1016/j.tifs.2014.09.003
  contributor:
    fullname: MM Yusoff
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Snippet The purpose of the present study was to increase the proteinase activity of the strain NCU116 by combining ultraviolet irradiation and N -methyl- N′ -nitro- N...
The purpose of the present study was to increase the proteinase activity of the strain NCU116 by combining ultraviolet irradiation and...
Abstract The purpose of the present study was to increase the proteinase activity of the strain NCU116 by combining ultraviolet irradiation and...
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StartPage 154
SubjectTerms Amylases
Aqueous enzymatic method
Bacillus amyloliquefacien
Biomedical and Life Sciences
Biotechnology
Calcium
Cellulase
Copper
Enzymatic properties
Enzymes
Extracellular enzymes
Extraction
Glucoamylase
Guanidine
Iron
Irradiation
Life Sciences
Microbial Genetics and Genomics
Microbiology
Milk
Mutagenesis
Oils & fats
Original
Original Article
Pectinase
Proteinase
Skim milk
Temperature effects
Ultraviolet radiation
UV and NTG mutation
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  providerName: Springer Nature
Title Mutagenesis and characterization of a Bacillus amyloliquefaciens strain for Cinnamomum camphora seed kernel oil extraction by aqueous enzymatic method
URI https://link.springer.com/article/10.1186/s13568-017-0451-9
https://www.ncbi.nlm.nih.gov/pubmed/28724263
https://www.proquest.com/docview/1922767208
https://pubmed.ncbi.nlm.nih.gov/PMC5514006
https://doaj.org/article/00de5f68748749dfa4ef681b309f2abe
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