Bovine serum chitinase
1 A glycol‐chitin‐splitting enzyme without lysozyme (muramidase) activity has been found in calf serum. The enzyme also degrades colloidal chitin and is thus a true chitinase, 1,4‐β‐poly‐N‐ acetylglucosaminidase, without exo‐β‐N‐acetylglucosaminidase effect. 2 The enzyme is purified 1000‐fold by ion...
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| Published in: | European journal of biochemistry Vol. 100; no. 2; pp. 455 - 460 |
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| Main Authors: | , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
Oxford, UK
Blackwell Publishing Ltd
01-01-1979
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| Subjects: | |
| Online Access: | Get full text |
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| Summary: | 1
A glycol‐chitin‐splitting enzyme without lysozyme (muramidase) activity has been found in calf serum. The enzyme also degrades colloidal chitin and is thus a true chitinase, 1,4‐β‐poly‐N‐ acetylglucosaminidase, without exo‐β‐N‐acetylglucosaminidase effect.
2
The enzyme is purified 1000‐fold by ion‐exchange chromatography and gel filtration. Its optimal activity is between pH 1.5 – 2.0 with glycol chitin and between pH 3 – 6 in a rather broad optimum with colloidal chitin as substrate.
The optimal stability of the enzyme is in the pH interval 3.0–6.5 when tested by incubation with glycol chitin at 50 °C for 60 min. The optimal temperature for the degradation of glycol chitin is 40°C when assayed at pH 1.5 and 51°C when assayed at pH 3.5.
3
The enzyme is activated by moderate heating at pH < 6.5. The highest relative activity, 135%, is reached after 45 rnin incubation at 30°C, pH 5 or after 30 rnin at 40°C, pH 2.4. By incubation with small amounts of trypsin at pH 6.5 at 37°C the enzyme was temporarily activated.
4
The isoelectric point, PI 5.3, and the molecular weight, 47000 ± 3000 were determined by respectively isoelectric focusing and gel filtration.
5
The Michaelis‐Menten constant, Km= 0.76 ± 0.05 (S.E.) mg/ml, was measured with glycol chitin as substrate. |
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| Bibliography: | L70 L ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| ISSN: | 0014-2956 1432-1033 |
| DOI: | 10.1111/j.1432-1033.1979.tb04188.x |