Characterization, amyloid formation, and immobilization of a novel SGNH hydrolase from Listeria innocua 11262

A novel oligomeric hydrolase (LI22) from Listeria innocua CLIP 11262 was identified, characterized, and immobilized for industrial application. Sequence analysis of LI22 revealed a putative catalytic triad (Ser10-Asp176-His179), and a conserved sequence motif Ser(S)10-Gly(G)77-Asn(N)79-His(H)179 wit...

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Veröffentlicht in:	International journal of biological macromolecules 2012-01, Vol.50 (1), p.103-111
Hauptverfasser:	Kim, Seulgi, Bae, Song Yi, Kim, Seung Joon, Ngo, Tri Duc, Kim, Kyeong Kyu, Kim, T. Doohun
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amyloid - chemistry Amyloid formation Carboxylic Ester Hydrolases - chemistry Catalysis Chromatography, Gel Circular Dichroism Cross-Linking Reagents - chemistry Crosslinked enzyme aggregates Enzymes, Immobilized - chemistry Escherichia coli - enzymology Hydrolysis Listeria - metabolism Models, Molecular Molecular Sequence Data Mutation Nitrophenols - chemistry Sequence Homology, Amino Acid SGNH hydrolase Spectrometry, Fluorescence - methods Thiazoles - chemistry
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Beschreibung
Zusammenfassung:	A novel oligomeric hydrolase (LI22) from Listeria innocua CLIP 11262 was identified, characterized, and immobilized for industrial application. Sequence analysis of LI22 revealed a putative catalytic triad (Ser10-Asp176-His179), and a conserved sequence motif Ser(S)10-Gly(G)77-Asn(N)79-His(H)179 with moderate identities (
ISSN:	0141-8130 1879-0003
DOI:	10.1016/j.ijbiomac.2011.10.003