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Title:A novel metalloprotease from Bacillus cereus for protein fibre processing
Authors:Sousa, Fernanda de (Author)
Jus, Suzana (Author)
Erbel, Anita (Author)
Kokol, Vanja (Author)
Cavaco-Paulo, Artur (Author)
Gübitz, Georg M. (Author)
Files:URL http://dx.doi.org/10.1016/j.enzmictec.2006.12.017
Work type:Unknown ()
Typology:1.01 - Original Scientific Article
Organization:FS - Faculty of Mechanical Engineering
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:textile finishing, enzymatic modification, wool fibre, enzymes, Bacilus cereus, specificity, kinetics, metalloprotease
Year of publishing:2007
ISSN on article:0141-0229
COBISS_ID:11072278 New window
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Record is a part of a journal

Title:Enzyme and microbial technology
Shortened title:Enzyme microb. technol.
Publisher:Butterworth Scientific Ltd
COBISS.SI-ID:25406976 New window

Secondary language

Keywords:plemenitenje tekstilij, enzimska modifikacija, volnena vlakna, encimi, Bacilus cereus, proteaze, specifičnost, kinetika, metaloproteaza


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