Effects of chemical modification on the stability of invertase before and after immobilization

被引:23
作者
Husain, S [1 ]
Jafri, F [1 ]
Saleemuddin, M [1 ]
机构
[1] ALIGARH MUSLIM UNIV,FAC LIFE SCI,DEPT BIOCHEM,ALIGARH 202001,UTTAR PRADESH,INDIA
关键词
invertase; immobilization; stabilization of invertase;
D O I
10.1016/0141-0229(95)00119-0
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Invertase from baker's yeast immobilized by coupling the amino acid side-chain amino groups or glycosyl residues to the matrix has been studied for its resistance to heat and urea-induced denaturation, to understand the influence of the nature of immobilization procedure on these processes. The possible role of chemical modifications and/or carbohydrate depletion to which the enzyme was subjected was also examined by investigating the properties of soluble modified enzyme. The immobilized preparations obtained were Sp-INV by direct coupling of invertase to Sepharose, Sp-PEA-INV by coupling of periodate and ethanolamine-treated invertase to Sepharose, Sp-PEDA-INV by coupling of periodate and ethylenediamine-treated invertase to Sepharose, and Sp-PEDA-2-4-6-trinitrobenzene sulfonic acid (TNBS)-INV by coupling of TNBS followed by periodate and ethylenediamine-treated invertase to Sepharose. All of the immobilized preparations exhibited higher stability against heat and urea-induced inactivation as compared to native invertase, Among the procedures employed for immobilization of invertase, the Sp-PEDA-INV preparation exhibited highest yield of immobilization, eta value, and thermal and storage stability. The yield of immobilization and stabilization was followed by Sp-PEA-INV, Sp-INV, and Sp-PEDA-TNBS-INV preparations.
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页码:275 / 280
页数:6
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