Study of the effects of temperature, pH and NaCl on the peptidase activities of non-starter lactic acid bacteria (NSLAB) by quadratic response surface methodology

被引:35
作者
Gobbetti, M
Lanciotti, R
De Angelis, M
Corbo, MR
Massini, R
Fox, PF
机构
[1] Univ Foggia, Fac Agr Foggia, Ist Prod & Preparaz Alimentari, I-71100 Foggia, Italy
[2] Fac Agr, Ist Ind Agr Microbiol, I-06426 Perugia, Italy
[3] Natl Univ Ireland Univ Coll Cork, Dept Food Chem, Cork, Ireland
关键词
cheese ripening; peptidase enzymes; non-starter lactic acid bacteria; quadratic response surface methodology;
D O I
10.1016/S0958-6946(99)00156-9
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The individual and interactive effects of temperature, pH and NaCl on the aminopeptidase-types N and A and proline iminopeptidase activities of several strains of non-starter lactic acid bacteria (NSLAB) were studied by quadratic response surface methodology. The effects on enzyme activities depended on the interactions among the independent variables, species, strains within species and type of activity. With few exceptions, the aminopeptidases N and A and proline iminopeptidase activities of Lactobacillus casei sap. pseudoplantarum and Lb. curvatus were strongly inhibited by the hostile cheese-like conditions, while the peptidases of Lb. casei ssp. casei and especially Lb. plantarum were tolerant or not affected by variations in pH and showed the least sensitivity to NaCl or even a requirement for NaCl for the optimal activity. Strains which maintained relatively high activity under cheese-like conditions were selected within the species. The proline iminopeptidase of Lb. casei ssp, casei 2107 as well as Lb. plantarum 2788 and 2789 greatly tolerated the interactions among the independent variables. At 10 degrees C in the presence of 3.750% NaCl and independent of the pH, the PepN activity of Lb. plantarum 2788 and 2789 was at least 33% of the maximum determined at pH 7.5 and 35 degrees C. Proline iminopeptidase activity was most sensitive to the individual and interactive variations in temperature, pH and NaCl. On the other hand, aminopeptidase-type A activity seemed to be least sensitive to cheese-like conditions. (C) 2000 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:865 / 875
页数:11
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