Journal ArticleOPEN ACCESS

Purification and some properties of a keratinolytic enzyme from an alkaliphilic nocardiopsis sp. TOA-1

Bioscience, Biotechnology and Biochemistry (2002) 66(1) 164-167
DOI: 10.1271/bbb.66.164
74Citations
Citations of this article
32Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

A novel alkaliphilic Nocardiopsis sp., strain TOA-1, was isolated from a tile-joint of a bathroom. Strain TOA-1 produced a variety of alkaline hydrolytic enzymes. An alkaline protease, designated NAPase, was purified and characterized. NAPase had a very high keratinolytic activity and high stability under acidic conditions. © 2002, Taylor & Francis Group, LLC. All rights reserved.

Author supplied keywords

Cite

CITATION STYLE

APA

Mitsuiki, S., Sakai, M., Moriyama, Y., Goto, M., & Furukawa, K. (2002). Purification and some properties of a keratinolytic enzyme from an alkaliphilic nocardiopsis sp. TOA-1. Bioscience, Biotechnology and Biochemistry, 66(1), 164–167. https://doi.org/10.1271/bbb.66.164

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free