| A STUDY OF ALGINATE LYASES Ⅰ. ISOLATION, PURIFICATION AND KINETICS OF LYASES |
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| 引用本文： | 朱仁华,蔡少玲,李红智.A STUDY OF ALGINATE LYASES Ⅰ. ISOLATION, PURIFICATION AND KINETICS OF LYASES[J].海洋学报(英文版),1987,6(2):281-291. |
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| 作者姓名： | 朱仁华 蔡少玲 李红智 |
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| 作者单位： | Jiaxing University，Shenzhen Fisheries Culture Company，Institute of Oceanology，Academic Sinica，Qingdao |
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| 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, KC1 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.
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| 收稿时间： | 1986/3/19 0:00:00 |
| 修稿时间： | 7/1/1986 12:00:00 AM |
A STUDY OF ALGINATE LYASES Ⅰ. ISOLATION,PURIFICATION AND KINETICS OF LYASES |
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| ZHU RENHUA,CAI SHAOLING and LI HONGZHI.A STUDY OF ALGINATE LYASES Ⅰ. ISOLATION,PURIFICATION AND KINETICS OF LYASES[J].Acta Oceanologica Sinica,1987,6(2):281-291. |
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| Authors: | ZHU RENHUA CAI SHAOLING and LI HONGZHI |
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| Institution: | 1.Jiaxing University2.Shenzhen Fisheries Culture Company3.Institute of Oceanology, Academic Sinica, Qingdao |
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| 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. |
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