Characterization of Ca2+ -activated cell-bound proteinase from Virgibacillus sp SK37 isolated from fish sauce fermentation
Characterization of Ca2+ -activated cell-bound proteinase from Virgibacillus sp SK37 isolated from fish sauce fermentation
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DOI：
10.1016/j.lwt.2008.02.002
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发表时间：
2008-12-01
影响因子：
6
通讯作者：
Yongsawatdigul, Hrawat
中科院分区：
文献类型：
--
作者：
Sinsuwan, Sornchai;Rodtong, Sureelak;Yongsawatdigul, Hrawat
对鱼露发酵第一个月分离的Virgibacillus sp. SK37细胞结合蛋白酶进行了鉴定。以偶氮酪蛋白为底物，在65℃、pH 7.0和9.5条件下酶活性最高。该酶至少需要10 mmol/l Ca2+才能有效水解酪蛋白，并且随着Ca2+浓度的增加，酪蛋白的降解程度增加。乙二胺四乙酸（EDTA）和苯甲磺酰氟（PMSF）显著抑制了丝氨酸蛋白酶的活性，表明Ca2+激活丝氨酸蛋白酶的特征。在所测试的6种合成底物中，该酶较好地水解了su - ala - ala - pro - ph - amc，表明该酶是一种枯草菌素样蛋白酶。虽然在20 g/100 ml NaCl条件下对肌动球蛋白的活性比在5 g/100 ml NaCl条件下降低到63%，但该酶在25 g/100 ml NaCl条件下，30℃条件下表现出很高的稳定性。这是首次报道从鱼露中分离的中等嗜盐细菌的细胞结合蛋白酶的生化特性。(C) 2008瑞士食品科学与技术学会。Elsevier Ltd.出版。版权所有。
Cell-bound proteinase from Virgibacillus sp. SK37 isolated from the first month of fish sauce fermentation was characterized. The enzyme showed the maximum activity at 65 degrees C, pH 7.0 and 9.5, using azocasein as a substrate. The enzyme required at least 10 mmol/l Ca2+ to effectively hydrolyze casein and the extent of casein degradation increased with Ca2+ concentration. Ethylenediaminetetraacetic acid (EDTA) and phenylmethanesulfonyl fluoride (PMSF) largely inhibited the activity, indicating a characteristic of Ca2+-activated serine proteinase. Among six synthetic substrates tested, the enzyme preferably hydrolyzed Suc-Ala-Ala-Pro-Phe-AMC, indicating a subtilisin-like proteinase. Although activity towards actomyosin at 20 g/100 ml NaCl decreased to 63% compared to at 5 g/100 ml, the enzyme showed high stability at 25 g/100 ml NaCl, 30 degrees C. This was the first study to report biochemical characteristics of cell-bound proteinase from a moderately halophilic bacterium isolated from fish sauce. (C) 2008 Swiss Society of Food Science and Technology. Published by Elsevier Ltd. All rights reserved.