PEPTIDE-HYDROLASES OF PROPIONIBACTERIA - EFFECT OF PH AND TEMPERATURE

被引:14
作者
CHAIA, AP
HOLGADO, APD
OLIVER, G
机构
[1] CTR REFERENCIA LACTOBACILOS,CHACABUCO 145,RA-4000 TUCUMAN,ARGENTINA
[2] NATL UNIV TUCUMAN,FAC BIOQUIM QUIM & FARM,TUCUMAN,ARGENTINA
关键词
D O I
10.4315/0362-028X-53.3.237
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A comparative study of the activity of peptidases belonging to the four classic propionibacteria species cultured in milk was carried out at different values of pH and temperature. Leucine aminopeptidase and proline iminopeptidase showed greater activity in Propionibacterium freudenreichii than in the other species studied. With the single exception of Propionibacterium jensenii, the propionibacteria peptidase tested exhibited greater affinity for proline than for leucine-p-nitroanilide. Optimum temperature and pH in relation to the activity of both substrates varied according to the species under consideration. Copyright © International Association of Miik, Food and Environmental Sanitarians.
引用
收藏
页码:237 / 240
页数:4
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