Purification and properties of a thermostable chitinase from Streptomyces thermoviolaceus OPC-520

H Tsujibo; K Minoura; K Miyamoto; H Endo; M Moriwaki; Y Inamori

doi:10.1128/aem.59.2.620-622.1993

Purification and properties of a thermostable chitinase from Streptomyces thermoviolaceus OPC-520

Appl Environ Microbiol. 1993 Feb;59(2):620-2. doi: 10.1128/aem.59.2.620-622.1993.

Authors

H Tsujibo¹, K Minoura, K Miyamoto, H Endo, M Moriwaki, Y Inamori

Affiliation

¹ Osaka University of Pharmaceutical Sciences, Japan.

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.

MeSH terms

Amino Acid Sequence
Chitinases / chemistry
Chitinases / isolation & purification*
Molecular Sequence Data
Sequence Homology, Amino Acid
Serratia marcescens / enzymology
Streptomyces / classification
Streptomyces / enzymology*

Substances

Chitinases