title: Purification and properties of a thermostable chitinase from Streptomyces thermoviolaceus OPC-520.
abstract: A chitinase was purified from the culture filtrate of Streptomyces thermoviolaceus OPC-520. The enzyme showed a high optimum temperature (70 to 80 degrees C), a high optimum pH level (8.0 to 10.0), and heat stability. This enzyme showed high sequence homology with chitinases from Serratia marcescens QMB1466 and Bacillus circulans WL-12.
authors.affiliation: Osaka University of Pharmaceutical Sciences, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Tsujibo
authors.forename: K
authors.initials: K
authors.lastname: Minoura
authors.forename: K
authors.initials: K
authors.lastname: Miyamoto
authors.forename: H
authors.initials: H
authors.lastname: Endo
authors.forename: M
authors.initials: M
authors.lastname: Moriwaki
authors.forename: Y
authors.initials: Y
authors.lastname: Inamori
mesh_terms: D000595:Amino Acid Sequence; D002688:Chitinases / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012706:Serratia marcescens / Q000201:enzymology; D013302:Streptomyces / Q000145:classification / Q000201:enzymology*
chemical_list: D002688:Chitinases