Purification and characterisation of an alkaline protease used in tannery industry from Bacillus licheniformis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2004-09

AUTHORS

Xue-Ming Tang, F.M. Lakay, Wei Shen, Wei-Lan Shao, Hui-Ying Fang, B.A. Prior, Zheng-Xiang Wang, Jian Zhuge

ABSTRACT

An extracellular alkaline protease produced by Bacillus licheniformis AP-1 was purified 76-fold, yielding a single 28 kDa band on SDS-PAGE. It was optimally active at pH 11 and at 60 degrees C (assayed over 10 min). The protease was completely inhibited by phenylmethylsulfonyl fluoride and diodopropyl fluorophosphate, with little increase upon Ca2+ and Mg2+ addition. More... »

PAGES

1421-1424

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/b:bile.0000045642.19299.3f

DOI

http://dx.doi.org/10.1023/b:bile.0000045642.19299.3f

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037225507

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15604774


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