地衣芽孢杆菌L-天冬酰胺酶I型的克隆表达及其在薯条中的应用

摘要/Abstract

摘要： 摘要：L-天冬酰胺酶可水解L-天冬酰胺，从而抑制高温加工食品中致癌物质丙稀酰胺的生成。为提高地衣芽孢杆菌L-天冬酰胺酶I型产量，将L-天冬酰胺酶I型酶基因克隆并实现其在大肠杆菌中表达。重组酶活力为63.64±3.18 IU/mL，比活力为945.79 IU/mg，最适催化反应条件为pH10.0，45 ℃。45 ℃处理12 h后，重组酶的残余酶活仍大于90%。该酶无谷氨酰胺催化能力，具有23.38%的D-天冬酰胺活性，其Km值为12.19 mM，最大反应速度Vmax为2.69 IU/mL。此外，将L-天冬酰胺酶I型应用于油炸薯条中，处理后的样品中丙烯酰胺含量降低58.39%。研究表明，地衣芽孢杆菌L-天冬酰胺酶I型具有应用于食品加工工业的潜力。

关键词: 关键词：L-天冬酰胺酶I型, 地衣芽孢杆菌, 酶学性质, 丙烯酰胺抑制, 薯条

Abstract: Abstract: L-asparaginases have the potential to inhibit the formation of acrylamide during food production. The type I L-asparaginase gene from Bacillus licheniformis was cloned and expressed in Escherichia coli. The recombined L-asparaginase had an activity of 63.64±3.18 IU/mL, and specific activity of the enzyme was 945.79 IU/mg. BlAase I exhibited maximum catalytic activity at pH 10.0 and 45 °C. The relative enzyme activity was maintained above 90 at 45 °C for 12 h. In addition to L-asparagine, BlAase I showed catalytic ability to D-asparagine, which was 23.38% of L-asparaginase activity. The Km value of BlAase I was 12.19 mM, and Vmax value was 2.69 IU/mL. Moreover, BlAase I had the ability to mitigate acrylamide formation in French fries. Compared with the untreated group, the acrylamide content in samples treated with BlAase I was effectively decreased by 58.39%. These results indicate that the novel type I L-asparaginase BlAase I has the potential for application in the food processing industry.

Key words: Keywords: L-asparaginase, Bacillus licheniformis, Characterization, Acrylamide mitigation, French fries

中图分类号:

TS201.3

陈菊花焦琳舒吕凤霞谢亚娟. 地衣芽孢杆菌L-天冬酰胺酶I型的克隆表达及其在薯条中的应用[J]. 食品科学, 0, (): 0-0.

Ju-Hua CHEN lu fengxia. Cloning,expression and characterization of a novel type I L-asparaginase from Bacillus licheniformis and its application in French fries[J]. FOOD SCIENCE, 0, (): 0-0.

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