Serratia marcescens chitinase: One-step purification and use for the determination of chitin |
| |
Authors: | Rowena L Roberts Enrico Cabib |
| |
Institution: | Section on Enzymes and Cellular Biochemistry, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20205 USA |
| |
Abstract: | 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-acetylglucosamine by traces of β-N-acetylglucosaminidase 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. |
| |
Keywords: | To whom correspondence should be addressed: National Institutes of Health Building 10/Room 9N-119 Bethesda Md 20205 |
本文献已被 ScienceDirect 等数据库收录! |
|