Characterization of a thermostable esterase activity from the moderate thermophile Bacillus licheniformis
Characterization of a thermostable esterase activity from the moderate thermophile Bacillus licheniformis
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DOI：
10.1271/bbb.63.1865
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发表时间：
1999-11-01
影响因子：
1.6
通讯作者：
Baratti, J
中科院分区：
文献类型：
--
作者：
Alvarez-Macarie, E;Augier-Magro, V;Baratti, J
从大肠杆菌重组菌株中分离到一种新的地衣芽孢杆菌酯酶活性。该蛋白为单链多肽，分子量为81 kDa。酶活的最适pH为8-8.5，在7-8.5范围内稳定。活性的最适温度为45 ℃，半衰期为64 ℃时1小时。最大的活动上观察到的对硝基苯基己酸酯的活动对长链脂肪酸酯。该酶在pH 8和37 ℃下水解己酸对硝基苯基酯的K-M为0.52mM。金属离子和巯基试剂均不影响酶的活性。令人惊讶的是，该酶仅被PMSF轻微抑制。这些特征将新酶归类为与脂肪酶具有相似性的热稳定酯酶。该酯酶可用于酯合成等生物技术应用。
A new esterase activity from Bacillus licheniformis was characterized from an Escherichia coli recombinant strain. The protein was a single polypeptide chain with a molecular mass of 81 kDa. The optimum pH for esterase activity was 8-8.5 and it was stable in the range 7-8.5. The optimum temperature for activity was 45 degrees C and the half-life was Ih at 64 degrees C. Maximum activity was observed on p-nitrophenyl caproate with little activity toward long-chain fatty acid esters. The enzyme had a K-M of 0.52 mM for p-nitrophenyl caproate hydrolysis at pH 8 and 37 degrees C. The enzyme activity was not affected by either metal ions or sulfydryl reagents. surprisingly, the enzyme was only slightly inhibited by PMSF. These characteristics classified the new enzyme as a thermostable esterase that shared similarities with lipases. The esterase might be useful for biotechnological applications such as ester synthesis.