热稳定性
米根霉
脂肪酶
克隆(编程)
大肠杆菌
根霉
基因
生物
生物化学
化学
酶
发酵
计算机科学
程序设计语言
作者
H. D. Beer,J. McCarthy,Uwe T. Bornscheuer,Roland M. Schmid
出处
期刊:Biochimica et biophysica acta (N)
[Elsevier]
日期:1998-08-20
卷期号:1399 (2-3): 173-180
被引量:65
标识
DOI:10.1016/s0167-4781(98)00104-3
摘要
A lipase from Rhizopus oryzae DSM 853 (ROL) was cloned from a chromosomal gene bank, sequenced and overexpressed in Escherichia coli. ROL and its precursors ProROL and PreProROL were purified and their pH and temperature profile was determined. In contrast to ROL, ProROL and PreProROL had considerably higher thermostability and a slightly higher pH optimum. Moreover, it could be demonstrated by in vitro experiments that the natural leader sequence of ROL is able to inhibit the folding supporting properties of the prosequence, resulting in a retardation of folding. In addition, there is strong evidence that all different lipase forms derived from Rhizopus sp. described in the literature are a result of different proteolytic processing and originate from the same gene.
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