Purification and characterization of CEP from Lactococcus lactis ssp lactis

被引：12
|
作者：
Guo, Yuxing [1 ]
Pan, Daodong [1 ]
Zeng, Xiaoqun [1 ]
Tanokura, Masaru [2 ]
机构：
[1] Nanjing Normal Univ, Dept Food Sci & Nutr, Nanjing 210097, Peoples R China
[2] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo 1138657, Japan
来源：
FOOD CHEMISTRY | 2009年 / 112卷 / 03期
关键词：
CEP; Purification and characterization; Whey protein hydrolysate; ACE-inhibitory activity; ANGIOTENSIN-CONVERTING ENZYME; WALL-ASSOCIATED PROTEINASE; CELL-ENVELOPE PROTEINASE; PROTEOLYTIC-ENZYMES; SPECIFICITY; PEPTIDES; SEQUENCE;
D O I：
10.1016/j.foodchem.2008.06.002
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
The cell-envelope proteinase (CEP) of Lactococcus lactis ssp. lactis LB12 was released from cells by treatment with lysozyme, purified by ammonium sulfate precipitation and chromatographed on DEAE-Sephadex A-25 and Sephacryl S-300 HR. The purified CEP is a monomer structure and has molecular mass of about 53 kDa. Optimal activity occurred at pH 7.5 and 40 degrees C. It is a metallopeptidase. activated by Mn2+, Mg2+, Ca2+, inhibited by Co2+, Zn2+, Ni2+ and EDTA, and a serine proteinase which is inhibited by PMSF. The sequence of the first 13 amino acids of the N-terminal of the CEP was determined to be Asp-Val-Phe-Ala-Pro-His-Met-Ala-Asn-Val-Ala-Ala-Val, and the whey protein hydrolysate produced by the CEP displayed ACE-inhibitory activity. (c) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码：533 / 538
页数：6
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