Purification and characterization of a rice class I chitinase, OsChia1b, produced in Esherichia coli.
To determine the properties and structure of OsChia1b, a family 19 chitinase from Oryza sativa L. cv. Nipponbare (japonica ssp.), recombinant OsChia1b was produced in Esherichia coli cells and purified to homogeneity by chitin affinity column chromatography. OsChia1b was highly active against soluble chitinous substrate, but not against crystalline chitin, and clearly inhibited hyphal extension of Trichoderma reesei.
Mizuno
Ryoji
R
Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, 8050 Ikarashi-2, Niigata 950-2181, Japan.
Itoh
Yoshikane
Y
Nishizawa
Yoko
Y
Kezuka
Yuichiro
Y
Suzuki
Kazushi
K
Nonaka
Takamasa
T
Watanabe
Takeshi
T
D002686:Chitin / Q000378:metabolism; D002688:Chitinases / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism / Q000502:physiology*; D003001:Cloning, Molecular; D029968:Escherichia coli Proteins / Q000235:genetics; D025301:Hyphae / Q000254:growth & development; D012275:Oryza / Q000201:enzymology*; D011487:Protein Conformation; D012995:Solubility; D013379:Substrate Specificity; D014242:Trichoderma / Q000276:immunology / Q000648:ultrastructure
D029968:Escherichia coli Proteins; D002686:Chitin; D002688:Chitinases; C094590:chitinase ChiA