Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/13561

TitleA novel metalloprotease from Bacillus cereus for protein fibre processing
Author(s)Sousa, Fernanda
Jus, S.
Erbel, Anita
Kokol, V.
Paulo, Artur Cavaco
Gübitz, Georg M.
KeywordsMetalloprotease
Specificity
Kinetics
Wool fibre
Issue dateJul-2007
PublisherElsevier
JournalEnzyme and Microbial Technology
Abstract(s)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.
TypeArticle
URIhttp://hdl.handle.net/1822/13561
DOI10.1016/j.enzmictec.2006.12.017
ISSN0141-0229
Publisher versionhttp://www.sciencedirect.com/science/article/pii/S0141022906006090
Peer-Reviewedyes
AccessOpen access
Appears in Collections:DET/2C2T - Artigos em revistas internacionais com arbitragem científica

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