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对Pcal_0917的结构和功能分析,Pcal_0917是一种来自超热友的古Pyrobaculum calidifontis的α-葡萄糖酶

Majida Atta Muhammad¹, Nasir Ahmad¹, Mohsina Akhter¹

¹School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore 54590, Pakistan.

International journal of biological macromolecules

|June 17, 2023

概括

来自Pyrobaculum calidifontis的新型酶Pcal_0917表现出高的α-葡萄糖酶活性. 这种热稳定酶在粉水解和葡萄糖糖生产中显示出工业应用的潜力.

科学领域:

酶学是一种酶学.
生物化学生物化学
微生物生物技术微生物生物技术

背景情况:

对Pyrobaculum calidifontis的基因组分析发现了一个α-葡萄糖酶基因 (Pcal_0917).
结构分析表明Pcal_0917属于II型α-葡萄糖酶.

研究的目的:

为了描述异质表达的Pcal_0917酶.
评估其生物化学特性和潜在的工业应用.

主要方法:

在大肠杆菌中Pcal_0917的异质表达.
生物化学测试以确定酶活性,最佳条件和稳定性.
循环二元化 (CD) 谱法用于结构分析.
用p-nitrophenyl α-D-glucopyranoside和马尔托斯进行酶活性测定.
粉水解测定与α-amylase结合使用.

主要成果:

重组Pcal_0917显示了I型α-葡萄糖酶的生化特征,与最初的结构预测不同.
该酶是四聚胺酶,在95°C和pH值6.0处最好地活跃,并且独立于金属离子.
在90°C的热处理时,活性增加了35%,在这种温度下,半衰期超过7小时.
Pcal_0917表现出异常高的p-nitrophenyl α-D-glucopyranosidase活性和转糖化能力.
与α-氨酶结合,它从粉中产生了含糖量超过40%的葡萄糖糖.

结论:

Pcal_0917是一种高度活性和热稳定的α-葡萄糖酶,具有独特的生化特性.
它的高催化效率和稳定性使其成为工业粉加工的有希望的候选者.
该酶产生高葡萄糖糖的能力需要进一步研究生物技术应用.

关键词:

功能分析是一种功能分析.不同类的表达式不同类的表达式超热友好型的考古学子皮罗巴库勒姆 (Pyrrobaculum calidifontis) 是一种有气质的植物.α-葡萄糖化酶的使用.

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