Secretion of a trypsin-like thiol protease by a new keratinolytic strain of Bacillus licheniformis

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

When cultured in feather-containing broth with a growth optimum of pH 7.0 and 47°C, a Bacillus licheniformis strain exhibited a high chicken feather-degrading activity. A trypsin-like protease was isolated from its ferment broth and was partially characterized. The enzyme was constitutively secreted and was highly active towards N-benzoyl-Phe-Val-Arg-p-nitroanilide as chromogenic substrate. Its pH optimum was 8.5 and it exhibited the highest activity at 52°C. Fractionation on Sephadex G-100 column revealed that its molecular mass was about 42 kDa. The enzyme, which is new for the genus Bacillus, is a thiol protease, as tosyl-L-phenylalanine chloromethyl ketone, tosyl-L-lysine chloromethyl ketone, phenylmethylsulfonyl fluoride and ethylenediamine tetraacetate did not inhibit it, while HgCl2 and para-chloromercuribenzoate lowered its activity.

Original languageEnglish
Pages (from-to)221-224
Number of pages4
JournalFEMS Microbiology Letters
Volume205
Issue number2
DOIs
Publication statusPublished - Dec 18 2001

Fingerprint

Feathers
ethylenediamine
S 2160
Sulfhydryl Compounds
Trypsin
Peptide Hydrolases
p-Chloromercuribenzoic Acid
Phenylmethylsulfonyl Fluoride
Chromogenic Compounds
Mercuric Chloride
Enzymes
Ketones
Phenylalanine
Bacillus
Lysine
Chickens
Growth
Bacillus licheniformis
sephadex
lysine chloromethyl ketone

Keywords

  • Bacillus licheniformis
  • Keratinase
  • Protease secretion

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

@article{a2d6efab2dc24977b14532efc5af5eaf,
title = "Secretion of a trypsin-like thiol protease by a new keratinolytic strain of Bacillus licheniformis",
abstract = "When cultured in feather-containing broth with a growth optimum of pH 7.0 and 47°C, a Bacillus licheniformis strain exhibited a high chicken feather-degrading activity. A trypsin-like protease was isolated from its ferment broth and was partially characterized. The enzyme was constitutively secreted and was highly active towards N-benzoyl-Phe-Val-Arg-p-nitroanilide as chromogenic substrate. Its pH optimum was 8.5 and it exhibited the highest activity at 52°C. Fractionation on Sephadex G-100 column revealed that its molecular mass was about 42 kDa. The enzyme, which is new for the genus Bacillus, is a thiol protease, as tosyl-L-phenylalanine chloromethyl ketone, tosyl-L-lysine chloromethyl ketone, phenylmethylsulfonyl fluoride and ethylenediamine tetraacetate did not inhibit it, while HgCl2 and para-chloromercuribenzoate lowered its activity.",
keywords = "Bacillus licheniformis, Keratinase, Protease secretion",
author = "M. Rozs and L. Manczinger and C. V{\'a}gv{\"o}lgyi and F. Kevei",
year = "2001",
month = "12",
day = "18",
doi = "10.1016/S0378-1097(01)00462-1",
language = "English",
volume = "205",
pages = "221--224",
journal = "FEMS Microbiology Letters",
issn = "0378-1097",
publisher = "Wiley-Blackwell",
number = "2",

}

TY - JOUR

T1 - Secretion of a trypsin-like thiol protease by a new keratinolytic strain of Bacillus licheniformis

AU - Rozs, M.

AU - Manczinger, L.

AU - Vágvölgyi, C.

AU - Kevei, F.

PY - 2001/12/18

Y1 - 2001/12/18

N2 - When cultured in feather-containing broth with a growth optimum of pH 7.0 and 47°C, a Bacillus licheniformis strain exhibited a high chicken feather-degrading activity. A trypsin-like protease was isolated from its ferment broth and was partially characterized. The enzyme was constitutively secreted and was highly active towards N-benzoyl-Phe-Val-Arg-p-nitroanilide as chromogenic substrate. Its pH optimum was 8.5 and it exhibited the highest activity at 52°C. Fractionation on Sephadex G-100 column revealed that its molecular mass was about 42 kDa. The enzyme, which is new for the genus Bacillus, is a thiol protease, as tosyl-L-phenylalanine chloromethyl ketone, tosyl-L-lysine chloromethyl ketone, phenylmethylsulfonyl fluoride and ethylenediamine tetraacetate did not inhibit it, while HgCl2 and para-chloromercuribenzoate lowered its activity.

AB - When cultured in feather-containing broth with a growth optimum of pH 7.0 and 47°C, a Bacillus licheniformis strain exhibited a high chicken feather-degrading activity. A trypsin-like protease was isolated from its ferment broth and was partially characterized. The enzyme was constitutively secreted and was highly active towards N-benzoyl-Phe-Val-Arg-p-nitroanilide as chromogenic substrate. Its pH optimum was 8.5 and it exhibited the highest activity at 52°C. Fractionation on Sephadex G-100 column revealed that its molecular mass was about 42 kDa. The enzyme, which is new for the genus Bacillus, is a thiol protease, as tosyl-L-phenylalanine chloromethyl ketone, tosyl-L-lysine chloromethyl ketone, phenylmethylsulfonyl fluoride and ethylenediamine tetraacetate did not inhibit it, while HgCl2 and para-chloromercuribenzoate lowered its activity.

KW - Bacillus licheniformis

KW - Keratinase

KW - Protease secretion

UR - http://www.scopus.com/inward/record.url?scp=0035910194&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035910194&partnerID=8YFLogxK

U2 - 10.1016/S0378-1097(01)00462-1

DO - 10.1016/S0378-1097(01)00462-1

M3 - Article

C2 - 11750806

AN - SCOPUS:0035910194

VL - 205

SP - 221

EP - 224

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

SN - 0378-1097

IS - 2

ER -