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Purification and characterization of a novel bacteriocin CAMT2 produced by Bacillus amyloliquefaciens isolated from marine fish Epinephelus areolatus  ( SCI-EXPANDED收录)   被引量:63

文献类型:期刊文献

英文题名:Purification and characterization of a novel bacteriocin CAMT2 produced by Bacillus amyloliquefaciens isolated from marine fish Epinephelus areolatus

作者:An, Junying[1];Zhu, Wenjuan[1];Liu, Ying[1];Zhang, Xuemei[1];Sun, Lijun[1];Hong, Pengzhi[1];Wang, Yaling[1];Xu, Chunhou[2];Xu, Defeng[1];Liu, Huanming[1]

机构:[1]Guangdong Ocean Univ, Key Lab Adv Proc Aquat Prod, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Higher Educ Inst,Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China;[2]Guangdong Ocean Univ, Coll Agr, Zhanjiang 524088, Peoples R China

年份:2015

卷号:51

起止页码:278

外文期刊名:FOOD CONTROL

收录:SCI-EXPANDED(收录号:WOS:000350538100038)、、WOS

基金:This work was financially supported by Guangdong Science and Technology Fund (S2011010000328), National High Technology Research and Development Program of China (863 Program) (No. 2013AA102201), the National Science Fund (No. 30279987) and Higher Educational Cultivation Program for Major Scientific Research Projects of Guangdong Ocean University (No. GDOU2013050205).

语种:英文

外文关键词:Bacteriocin; Purification; Antimicrobial activity; Food biopreservative

外文摘要:A novel bacteriocin named CAMT2 was produced by strain ZJHD3-06 which was isolated from the marine fish Epinephelus areolatus and identified as Bacillus amyloliquefaciens, Bacteriocin CAMT2 inhibits important food spoilage and food-borne pathogens such as Listeria monocytogenes, Staphylococcus aureus, Escherichia coli and Vibrio parahaemolyticus. Bacteriocin CAMT2 was purified by ammonium sulfate precipitation, gel filtration chromatography on Sephadex G-50 and reversed phase chromatography on a C-18 column. The molecular mass of the purified bacteriocin CAMT2 was about 20.0 kDa and N-terminal sequencing of the peptides revealed low similarity with existing antimicrobial peptides, as determined by an LC MS/MS system. Bacteriocin CAMT2 was resistant for up to 100 degrees C and pH ranging 2-10, but lost its activity when treated with protease K. The bacteriocin also showed significant antimicrobial activity against L monocytogenes in a meat model system. These obtained results suggest that bacteriocin CAMT2 has potential for use as a food biopreservative. (C) 2014 Elsevier Ltd. All rights reserved.

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