Secretory expression in Bacillus subtilis, purification and characterization of a persistent protein-degrading enzyme from Nocardiopsis sp. TOA-1.

IF 1.4 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

Bioscience, Biotechnology, and Biochemistry Pub Date : 2024-12-10 DOI:10.1093/bbb/zbae191

Aoto Takano, Mamiko Yano, Tomoka Nakamura, Kazufumi Takano, Shun-Ichi Tanaka

引用次数: 0

Abstract

Keratinase from Nocardiopsis sp. TOA-1 (NAPase) holds significant potential for industrial and medical applications. Here, we developed a heterologous secretory expression system for NAPase in Bacillus subtilis. The recombinant enzyme exhibited catalytic properties comparable to the native enzyme, demonstrating its suitability for further protein engineering. This work provides a foundation for enhancing NAPase activity and stability, expediting its biotechnological applications.

查看原文本刊更多论文

枯草芽孢杆菌分泌表达、Nocardiopsis sp. TOA-1持久性蛋白降解酶的纯化和特性研究。

Nocardiopsis sp.的角化酶TOA-1 （NAPase）在工业和医学应用中具有重要的潜力。本研究在枯草芽孢杆菌中建立了NAPase的异源分泌表达系统。重组酶表现出与天然酶相当的催化性能，表明其适合进一步的蛋白质工程。本研究为提高NAPase活性和稳定性，加快其生物技术应用奠定了基础。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Bioscience, Biotechnology, and Biochemistry 生物-生化与分子生物学

CiteScore

3.50

自引率

0.00%

发文量

183

审稿时长

1 months

期刊介绍： Bioscience, Biotechnology, and Biochemistry publishes high-quality papers providing chemical and biological analyses of vital phenomena exhibited by animals, plants, and microorganisms, the chemical structures and functions of their products, and related matters. The Journal plays a major role in communicating to a global audience outstanding basic and applied research in all fields subsumed by the Japan Society for Bioscience, Biotechnology, and Agrochemistry (JSBBA).