Characterization of a keratinolytic serine protease from Bacillus subtilis KS-1

Hyung Joo Suh, Hyo K. Lee

Research output: Contribution to journalArticle

Abstract

A keratinolytic enzyme produced by Bacillus subtilis KS-1 isolated from poultry waste was purified and characterized using ultrafiltration, DEAE-Sephadex, and Sephadex G-100 chromatographies. The specific activity of the purified protease was 538.2 units/mg. The enzyme was shown to have a relative molecular mass of 25.4 kDa. The enzyme was made completely inactive by PMSF, which indicates a serine-protease. Dithiothreitol enhanced keratinolytic activity by 1.6 times at a concentration of 5.0 mM. These results suggest that the cleavage of the disulfide bonds with reducing agents can occur directly or by excretion of sulfite, which causes the sulfitolysis of the disulfide bonds. The first 10 amino acids of the N-terminal sequence are Ala-Gin-Pro-Val-Glu-Trp-Gly-Ile-Ser-Gln. The enzyme hydrolyzed casein and feather, but hydrolyzed casein more effectively than it did feather.

Original languageEnglish
Pages (from-to)165-169
Number of pages5
JournalJournal of Protein Chemistry
Volume20
Issue number2
DOIs
Publication statusPublished - 2001 Sep 21

Fingerprint

Serine Proteases
Bacilli
Bacillus subtilis
Feathers
Enzymes
Caseins
Disulfides
DEAE-Dextran
Sulfites
Poultry
Dithiothreitol
Reducing Agents
Ultrafiltration
Molecular mass
Chromatography
Peptide Hydrolases
Amino Acids

Keywords

  • Bacillus subtilis
  • Keratinolytic activity
  • Serine-protease

ASJC Scopus subject areas

  • Biochemistry

Cite this

Characterization of a keratinolytic serine protease from Bacillus subtilis KS-1. / Suh, Hyung Joo; Lee, Hyo K.

In: Journal of Protein Chemistry, Vol. 20, No. 2, 21.09.2001, p. 165-169.

Research output: Contribution to journalArticle

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