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Title: Catalytic activity of an immobilized α-amylase on mesoporous silicas
Authors: Mody, H M
Mody, K H
Jasra, R V
Shin, Hyuan June
Ryong, Ryoo
Issue Date: Sep-2002
Publisher: NISCAIR-CSIR, India
Abstract: Three silica supports, namely SBA15, silica-N and silica-AC, having different pore size distribution have been hydrothermally synthesized. α-Amylase, used for hydrolysis of starch, has been immobilized after amino functionalization of silica surface by covalent bonding through glutaraldehyde. The silica, before and after modification, has been characterized by XRD analysis, BET surface area and BJH pore size distribution by N2 sorption at 77 K. SBA15 and modified SBA15show ordered hexagonal structure, whereas the other two silica samples, viz., silica-N and silica-AC are found to be XRD amorphous. Pore size distribution of the studied silica ranges from 76 to 300Å. Amino functionalization and enzyme immobilization result in a decrease in surface area, pore volume and pore size for all the samples. On SBA15 and silica-N, enzyme immobilization is on external surface only, whereas on silica-AC, internal pores are found to be accessible to the enzyme molecules. Specific activity of α-amylase has been observed to follow the order silica-AC > silica-N > SBA15. Immobilized α-amylase exhibits higher operational stability in the order of SBA15 > silica-AC > silica-N. Immobilized α-amylase exhibits comparatively less specific activity than that of the free enzyme.
Page(s): 1795-1803
ISSN: 0975-0975(Online); 0376-4710(Print)
Appears in Collections:IJC-A Vol.41A(09) [September 2002]

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