| ZHU RENHUA,CAI SHAOLING,LI HONGZHI. 1987. A STUDY OF ALGINATE LYASES Ⅰ. ISOLATION, PURIFICATION AND KINETICS OF LYASES. Acta Oceanologica Sinica, (2):281－291 |
| A STUDY OF ALGINATE LYASES Ⅰ. ISOLATION, PURIFICATION AND KINETICS OF LYASES |
| A STUDY OF ALGINATE LYASES Ⅰ. ISOLATION, PURIFICATION AND KINETICS OF LYASES |
| Received:March 19, 1986 Revised:July 01, 1986 |
| DOI： |
| Key words: |
| 中文关键词: |
| 基金项目: |
|
| Hits: 687 |
| Download times: 564 |
| Abstract: |
The crude enzyme, which was extracted from viscera of Lunella coronata coreensis (Recluz), was salted out and dialysed. Three enzymatic peaks isolated from DEAE-cellulose column chromatography were refered to as lyase Ⅰ, Ⅱ and Ⅲ, respectively. Then these lyases underwent gel-filtration on Sephadex G-25 respectively, and three purer lyases were derived therefrom, the highest purification being 73 fold.
The kinetics of the three lyases was tested respectively. The optimum pH was as follows:lyase Ⅰ was 7.6±0.02 Tris-HCl buffer; lyase Ⅱ was 6.6±0.02 Na2HPO4-NaH2PO4 buffer; and lyase Ⅲ was 5.6±0.02 HAc-NaAc buffer. In the rang of tested concentration, KCl and Nad were the activator and MnCl2 was the inhibitor, all for the three lyases; MgCl2 was the activator for lyases Ⅰ and Ⅱ, but the MgCl2 of high concentration was the inhibitor for lyase Ⅲ; Pb (OAc)2 acted differently for three lyases. The Km values of these lyases were 0.2, 0.6 and 0.04 mg/ml in order of precedence. |
| 中文摘要: |
The crude enzyme, which was extracted from viscera of Lunella coronata coreensis (Recluz), was salted out and dialysed. Three enzymatic peaks isolated from DEAE-cellulose column chromatography were refered to as lyase Ⅰ, Ⅱ and Ⅲ, respectively. Then these lyases underwent gel-filtration on Sephadex G-25 respectively, and three purer lyases were derived therefrom, the highest purification being 73 fold.
The kinetics of the three lyases was tested respectively. The optimum pH was as follows:lyase Ⅰ was 7.6±0.02 Tris-HCl buffer; lyase Ⅱ was 6.6±0.02 Na2HPO4-NaH2PO4 buffer; and lyase Ⅲ was 5.6±0.02 HAc-NaAc buffer. In the rang of tested concentration, KCl and Nad were the activator and MnCl2 was the inhibitor, all for the three lyases; MgCl2 was the activator for lyases Ⅰ and Ⅱ, but the MgCl2 of high concentration was the inhibitor for lyase Ⅲ; Pb (OAc)2 acted differently for three lyases. The Km values of these lyases were 0.2, 0.6 and 0.04 mg/ml in order of precedence. |
|
HTML
View Full Text
View/Add Comment Download reader |
| Close |
|
|
|
