| Autor: |
Alfonso, Carlos, Martínez, M. Jesús, Reyes, Fuensanta |
| Zdroj: |
FEMS Microbiology Letters; August 1992, Vol. 95 Issue: 2-3 p187-187, 1p |
| Abstrakt: |
From autolysed cultures of Mucor rouxii, two chitosanases, A and B, were purified to electrophoretic homogeneity. Apparent Mr values of 76 000 and 58 000 and pI values of 4.9 and 4.7 were determined for A and B, respectively. Both chitosanases showed a high specificity for chitosan and chitosan derivatives. They had optimum activities at pH 5.0 and at temperatures of 55°C and 50°C for A and B, respectively. Enzyme A was inhibited by acetate ions and enzyme B by high substrate concentration. Both enzymes showed an endo-splitting type of activity, and the end product of chitosan degradation contained a mixture of dimer, trimer and higher molecular mass oligomers of glucosamine. Glucosamine oligosaccharides were poorly hydrolysed by these enzymes. Both enzymes extensively degraded the chitosan extracted from M. rouxii cell walls. |
| Databáze: |
Supplemental Index |
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