A thermostable esterase activity from newly isolated moderate thermophilic bacterial strains

被引:43
作者
Kademi, A [1 ]
Aït-Abdelkader, N [1 ]
Fakhreddine, L [1 ]
Baratti, JC [1 ]
机构
[1] Univ Aix Marseille 2, Fac Sci Luminy, Biocatalysis & Fine Chem Grp, F-13288 Marseille 9, France
关键词
esterase; lipase; thermophile; bacterium; thermostability;
D O I
10.1016/S0141-0229(98)00127-6
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
Thirty-nine bacterial moderate thermophilic strains growing on triolein as sole carbon and energy source were isolated from soil samples by an enrichment culture on a mineral medium. When grown on a Tween 80 medium, most of the strains showed very high specific growth rates in the range of 1-2 h(-1) which corresponded to doubling times of 20-40 min. A high esterase activity was detected in the cell culture of all strains when assayed on soluble p-nitrophenyl caprylate (pNPC8). Strain MAS2 showed the highest esterase activity (around 40 U l(-1)). This activity was equally recovered in the culture supernatant and cell fraction. The majority of the cell esterase activity was recovered in the supernatant after high speed centrifugation, suggesting a soluble localization. Activity on pNPC16 was only recovered in the high speed centrifugation pellet, suggesting a membrane localization for the lipase activity. The best medium for pNPC8 production was a synthetic medium containing both glucose and yeast extract. The culture medium supernatant showed the highest activity on p-nitrophenyl acetate (pNPC2) than on pNPC8 and no activity an pNPC16, indicating the presence of esterase rather than lipase activity. This pNPC8 activity was stable (98%) after a 1 h treatment at 70 degrees C which renders this new esterase very attractive for biotechnological applications. (C) 1999 Elsevier Science Inc.
引用
收藏
页码:332 / 338
页数:7
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