用于脂肪酶固定化的与脂肪酶融合的纤维素结合结构域的评估。

Evaluation of cellulose-binding domain fused to a lipase for the lipase immobilization.

作者信息

Hwang Sangpill, Ahn Jungoh, Lee Sumin, Lee Tai Gyu, Haam Seungjoo, Lee Kangtaek, Ahn Ik-Sung, Jung Joon-Ki

机构信息

Department of Chemical Engineering, Yonsei University, Seoul 120-749, Korea.

出版信息

Biotechnol Lett. 2004 Apr;26(7):603-5. doi: 10.1023/b:bile.0000021964.69500.6f.

DOI:10.1023/b:bile.0000021964.69500.6f

PMID:15168862

Abstract

A cellulose-binding domain (CBD) fragment of a cellulase gene of Trichoderma hazianum was fused to a lipase gene of Bacillus stearothermophilus L1 to make a gene cluster for CBD-BSL lipase. The specific activity of CBD-BSL lipase for oil hydrolysis increased by 33% after being immobilized on Avicel (microcrystalline cellulose), whereas those of CBD-BSL lipase and BSL lipase decreased by 16% and 54%, respectively, after being immobilized on silica gel. Although the loss of activity of an enzyme immobilized by adsorption has been reported previously, the loss of activity of the CBD-BSL lipase immobilized on Avicel was less than 3% after 12 h due to the irreversible binding of CBD to Avicel.

摘要

将哈茨木霉纤维素酶基因的纤维素结合结构域（CBD）片段与嗜热脂肪芽孢杆菌L1的脂肪酶基因融合，构建了CBD-BSL脂肪酶基因簇。将CBD-BSL脂肪酶固定在微晶纤维素（Avicel）上后，其水解油脂的比活性提高了33%，而将CBD-BSL脂肪酶和BSL脂肪酶固定在硅胶上后，其比活性分别降低了16%和54%。虽然此前已有报道吸附固定化酶会导致活性损失，但由于CBD与Avicel的不可逆结合，固定在Avicel上的CBD-BSL脂肪酶在12小时后的活性损失小于3%。