Biochemical properties of a chitin-binding class III chitinase in pumpkin leaves

When we compared the chitinase activity of various plant sources using colorimetric or active gel-staining assay methods, the specific activity of pumpkin leaves was the highest among the samples we analyzed. The highly active chitinase from pumpkin leaves (designated PL-ChtIII) was purified to homogeneity using affinity chitin gel and HPLC Mono-Q anion-exchange column chromatographies, In contrast to other members of the class III chitinase family, PL-ChtIII showed a strong binding affinity to the regenerated chitin gel column. The apparent molecular weight of PL-ChtIII was estimated to be 29 kDa on SDS-PAGE gel, while its optimum pH and temperature were shown to be pH 6.0 and 60 degrees C, respectively. Analyzing the reaction products of PL-ChtIII with swollen chitin as substrate, the dimer and tetramer of N-acetylglucosamine were produced as major products in the first hour of the enzymatic reaction along with a small amount of monomers and trimers, As the reaction time increased, dimeric N-acetylglucosamine became the predominant form of reaction product.
Publisher
SPRINGER-VERLAG SINGAPORE PTE LTD
Issue Date
1999-11
Language
ENG
Keywords

PATHOGENESIS-RELATED PROTEINS; BEAN-LEAVES; WHEAT-GERM; ETHYLENE; ENDOCHITINASE; PURIFICATION; TOBACCO; CLONING; GENES

Citation

JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.32, no.6, pp.541 - 546

ISSN
1225-8687
URI
http://hdl.handle.net/10203/74859
Appears in Collection
BS-Journal Papers(저널논문)
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