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Serratia marcescens chitinase: One-step purification and use for the determination of chitin

โœ Scribed by Rowena L. Roberts; Enrico Cabib

Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
849 KB
Volume
127
Category
Article
ISSN
0003-2697

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โœฆ Synopsis

The extracellular chitinase produced by Serratia marcescens was obtained in highly purified form by adsorption-digestion on chitin. After gel electrophoresis in a nondenaturing system, the purified preparation exhibited two major protein bands that coincided with enzymatic activity. A study of the enzyme properties showed its suitability for the analysis of chitin. Thus, the chitinase exhibited excellent stability, a wide pH optimum, and linear kinetics over a much greater range than similar enzymes from other sources. The major product of chitin hydrolysis was chitobiose, which was slowly converted into free N-acetylghtcosamine by traces of P-Nacetylghrcosaminidase present in the purified preparation. The preparation was free from other polysaccharide hydrolases. Experiments with radiolabeled yeast cell walls showed that the chitinase was able to degrade wall chitin completely and specifically.

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