Fine separation and characterization of Candida rugosa lipase isoenzymes
Fine separation and characterization of Candida rugosa lipase isoenzymes
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DOI：
10.1002/1521-4028(200210)42:5
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发表时间：
2002-10
影响因子：
3.1
通讯作者：
J. Xin;Yi Xu Xiao‐xue Hu;J. Cui;Shu-ben Li;Chun‐gu Xia;Li-Min Zhu
中科院分区：
文献类型：
--
作者：
J. Xin;Yi Xu Xiao‐xue Hu;J. Cui;Shu-ben Li;Chun‐gu Xia;Li-Min Zhu
Commercial Candida rugosa lipase has been separated into two distinct fractions (CRLA and CRLB) by anion‐exchange chromatography. As analyzed on SDS‐polyacrylamide gel electrophoresis, CRLA and CRLB are homogenous. At high ionic strength, CRLA and CRLB have similar hydrophobicity and UV spectra, suggesting that the open extent of the large hydrophobic pockets of CRLA and CRLB may be similar. At low ionic strength, using “hydrophobic interfacial affinity chromatography”, both CRLA and CRLB have been separated into four isofractions. They have different hydrophobicity and UV spectra, suggesting that the open extent of the large hydrophobic pocket of the four forms may be different. Further, the conversion of CRL isoenzymes in the process of organic solvent treatment and ester hydrolysis were examined. The results clearly showed not only that CRLB had been converted to CRLA, but also that CRLA sub‐fractions with different open extent of large hydrophobic pocket had been converted
