Screening of strains of lactococci isolated from Egyptian dairy products for their proteolytic activity

被引：47

作者：

El-Ghaish, Shady ^{[1
]}

Dalgalarrondo, Michele ^{[1
]}

Choiset, Yvan ^{[1
]}

Sitohy, Mahmoud ^{[1
,2
]}

Ivanova, Iskra ^{[3
]}

Haertle, Thomas ^{[1
]}

Chobert, Jean-Marc ^{[1
]}

机构：

[1] INRA, UR 1268, F-44300 Nantes, France

[2] Zagazig Univ, Fac Agr, Dept Biochem, Zagazig, Egypt

[3] Univ Sofia, Dept Gen & Appl Microbiol, Sofia, Bulgaria

来源：

FOOD CHEMISTRY | 2010年 / 120卷 / 03期

关键词：

LAB; Lactococcus; Cheese; Proteolysis; LACTIC-ACID BACTERIA; LACTOBACILLUS-DELBRUECKII; ENTEROCOCCUS-FAECALIS; BOUND PROTEINASE; CHEESE; HYDROLYSIS; MILK; EXOPOLYSACCHARIDES; PURIFICATION; ACIDOPHILUS;

D O I：

10.1016/j.foodchem.2009.11.007

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

A collection of cocci isolates (293) obtained from traditional Egyptian dairy products collected from four Egyptian regions yielded 151 lactic acid bacteria (LAB) cocci isolates. Among them, 24 isolates were characterised as highly proteolytic. SIDS-PAGE showed that 6 isolates were the most proteolytically active, which were classified into Enterococcus faecalis HH22 (4 isolates) and Enterococcus faecium DO623 (2 isolates). The proteolytic activity of E. faecalis was higher than that of E. faecium (particularly on beta-casein). The maximal degradation of milk proteins was achieved at pH 6.5-7.2 (E. faecalis) or pH 6.5 (E. faecium) and at 42 degrees C for both strains. The proteolytic activities of the two strains were inhibited mostly by the presence of EDTA, showing that their proteases belong mainly to metalloproteases. A slight inhibition of proteolysis by PMSF in the case of E. faecalis HH22 suggests a limited inclusion of serine proteases in its protease system. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：758 / 764

页数：7

共 27 条

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