Fernanda de Sousa (Author), Suzana Jus (Author), Anita Erbel (Author), Vanja Kokol (Author), Artur Cavaco-Paulo (Author), Georg M. Gübitz (Author)

Abstract

A novel protease produced by Bacillus cereus grown on wool as carbon and nitrogen source was purified. B. cereus protease is a neutral metalloprotease with a molecular mass of 45.6 kDa. The optimum activity was at 45 °C and pH 7.0. The substrate specificity was assessed using oxidized insulin B-chain and synthetic peptide substrates. The cleavage of the insulin B-chain was determined to be Asn3, Leu6, His10-Leu11, Ala14, Glu21, after 12 h incubation. Among the peptide substrates, the enzyme did not exhibit activity towards ester substrates; with p-nitroanilide, the kinetic data indicate that aliphatic and aromatic amino acids were the preferred residues at the P1 position. For furylacryloyl peptides substrates, which are typical substrates for thermolysin, the enzyme exhibited high hydrolytic activity with a Km values of 0.858 and 2.363 mM for N-(3-[2-Furyl]acryloyl)-Ala-Phe amide and N-(3-[2-Furyl]acryloyl)-Gly-Leu amide, respectively. The purified protease hydrolysed proteins substrates such as azocasein, azocoll, keratin azure and wool.

Keywords

plemenitenje tekstilij;enzimska modifikacija;volnena vlakna;encimi;Bacilus cereus;proteaze;specifičnost;kinetika;metaloproteaza;textile finishing;enzymatic modification;wool fibre;enzymes;specificity;kinetics;metalloprotease;

Data

Language: English
Year of publishing:
Typology: 1.01 - Original Scientific Article
Organization: UM FS - Faculty of Mechanical Engineering
UDC: 677.31.027.6:577.15
COBISS: 11072278 Link will open in a new window
ISSN: 0141-0229
Views: 1569
Downloads: 89
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Other data

Secondary language: English
Secondary keywords: plemenitenje tekstilij;enzimska modifikacija;volnena vlakna;encimi;Bacilus cereus;proteaze;specifičnost;kinetika;metaloproteaza;
URN: URN:SI:UM:
Pages: str. 1772-1781
Volume: ǂVol. ǂ40
Issue: ǂiss. ǂ7
Chronology: Jun. 2007
ID: 8718649
Recommended works:
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, Pub. No.: WO/2009/051569; International Application No.: PCT/SI2008/000054; Publication Date: 23.04.2009; International Filing Date: 17.10.2008