Document Detail

Purification and characterization of extracellular chin deacetylase from Colletotrichum lindemuthianum.
MedLine Citation:
PMID:  8987657     Owner:  NLM     Status:  MEDLINE    
Chitin deacetylase, active in the presence of acetate (96% of the enzymatic activity was retained in the presence of 100 mM sodium acetate), was purified to electrophoretic homogeneity from a culture filtrate of Colletotrichum lindemuthianum (944-fold with a recovery of 4.05%). The enzyme was induced in the medium after the eighth day of incubation simultaneously with the blackening of the medium. The molecular mass of the enzyme was 31.5 kDa and 33 kDa as judged by SDS-PAGE and gel filtration, respectively, suggesting that the enzyme is a single polypeptide. The optimum temperature was 60 degrees C and the optimum pH was 11.5-12.0 when glycol chitin was used as substrate. The enzyme was active toward glycol chitin, partially N-deacetylated water soluble chitin, and chitin oligomers the degrees of polymerization of which were more than four, but was less active with chitin trimer and dimer, and inactive with N-acetylglucosamine. The Km and kcat for glycol chitin were 2.55 mM and 27.1 s-1, respectively, and those for chitin pentamer were 414 microM and 83.2 s-1, respectively. The reaction rates of the enzyme toward glycol chitin and chitin oligomers seemed to follow the Michaelis-Menten kinetics.
K Tokuyasu; M Ohnishi-Kameyama; K Hayashi
Related Documents :
16763977 - Antihypertensive activity of chitin derivatives.
11525997 - Identification and characterization of a chitinase antigen from pseudomonas aeruginosa ...
2879847 - Topography of cell wall lytic enzyme in chlamydomonas reinhardtii: form and location of...
15050837 - The extracellular constitutive production of chitin deacetylase in metarhizium anisopli...
1672127 - Purification and properties of tryptophan-sensitive 3-deoxy-d-arabino-heptulosonate-7-p...
18481217 - Decolorization and detoxication of reactive industrial dyes by immobilized fungi tramet...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  60     ISSN:  0916-8451     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  1996 Oct 
Date Detail:
Created Date:  1997-02-27     Completed Date:  1997-02-27     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  1598-603     Citation Subset:  B    
Biomaterials Conversion Laboratory, National Food Research Institute, Ibaraki, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amidohydrolases / biosynthesis,  isolation & purification*
Chitin / analogs & derivatives*,  chemistry
Enzyme Induction
Hydrogen-Ion Concentration
Mitosporic Fungi / enzymology*
Molecular Structure
Reg. No./Substance:
1398-61-4/Chitin; 9012-76-4/Chitosan; 9056-32-0/glycolchitin; EC 3.5.-/Amidohydrolases; EC deacetylase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Isolation and analysis of cinnamic acid 4-hydroxylase homologous genes from a hybrid aspen, Populus ...
Next Document:  Efficient L-serine production from methanol and glycine by resting cells of Methylobacterium sp. str...