Immobilization of Beta-Glycosidase BglX from Escherichia coli on Chitosan Gel Beads

Immobilization of Beta-Glycosidase BglX from Escherichia coli on Chitosan Gel Beads

Bibliographic Details
Main Author: Pickens, Tara L., L
Language:English
Published: Youngstown State University / OhioLINK 2018
Subjects:
Biochemistry
Chemistry
Food Science
enzyme immobilization
chitosan
chitosan gel beads
glycoside hydrolase
beta-glycosidase
lactose hydrolysis
BglX
galactosidase
Online Access:http://rave.ohiolink.edu/etdc/view?acc_num=ysu1535472543349818
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spelling ndltd-OhioLink-oai-etd.ohiolink.edu-ysu15354725433498182021-08-03T07:08:29Z Immobilization of Beta-Glycosidase BglX from Escherichia coli on Chitosan Gel Beads Pickens, Tara L., L Biochemistry Chemistry Food Science enzyme immobilization chitosan chitosan gel beads glycoside hydrolase beta-glycosidase lactose hydrolysis BglX galactosidase Enzyme immobilization refers to any technique by which an enzyme is restrained or localized to a support system. This can provide retention of catalytic activity and reusability of the enzyme, both of which are important in industrial processes. Enzyme supports can be made of organic materials, typically naturally occurring polysaccharides, such as cellulose, agarose, or chitosan. The objective of this study was to immobilize beta glycosidase BglX and its mutant E293Q on chitosan gel beads while retaining catalytic activity. The beads were fortified with activated charcoal or silica and cross-linked with glutaraldehyde to increase their mechanical stability and immobilization efficiency. Lactase was used as a model enzyme to determine which type of chitosan gel bead was the most suitable for immobilization. The chromogenic substrate ortho-nitrophenyl ß-D-galactopyranoside (oNPGal) and a lactose solution were used to test the catalytic activity of immobilized lactase. Upon successfully immobilizing lactase, BglX and E293Q were tested similarly. Since BglX showed higher percent conversion of substrate, it was used in a packed bed column and the ability of the immobilized enzyme to hydrolyze the lactose present in milk whey was tested in a small-scale continuous production system. 2018-08-30 English text Youngstown State University / OhioLINK http://rave.ohiolink.edu/etdc/view?acc_num=ysu1535472543349818 http://rave.ohiolink.edu/etdc/view?acc_num=ysu1535472543349818 unrestricted This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws.
collection NDLTD
language English
sources NDLTD
topic Biochemistry
Chemistry
Food Science
enzyme immobilization
chitosan
chitosan gel beads
glycoside hydrolase
beta-glycosidase
lactose hydrolysis
BglX
galactosidase
spellingShingle Biochemistry
Chemistry
Food Science
enzyme immobilization
chitosan
chitosan gel beads
glycoside hydrolase
beta-glycosidase
lactose hydrolysis
BglX
galactosidase
Pickens, Tara L., L
Immobilization of Beta-Glycosidase BglX from Escherichia coli on Chitosan Gel Beads
author Pickens, Tara L., L
author_facet Pickens, Tara L., L
author_sort Pickens, Tara L., L
title Immobilization of Beta-Glycosidase BglX from Escherichia coli on Chitosan Gel Beads
title_short Immobilization of Beta-Glycosidase BglX from Escherichia coli on Chitosan Gel Beads
title_full Immobilization of Beta-Glycosidase BglX from Escherichia coli on Chitosan Gel Beads
title_fullStr Immobilization of Beta-Glycosidase BglX from Escherichia coli on Chitosan Gel Beads
title_full_unstemmed Immobilization of Beta-Glycosidase BglX from Escherichia coli on Chitosan Gel Beads
title_sort immobilization of beta-glycosidase bglx from escherichia coli on chitosan gel beads
publisher Youngstown State University / OhioLINK
publishDate 2018
url http://rave.ohiolink.edu/etdc/view?acc_num=ysu1535472543349818
work_keys_str_mv AT pickenstarall immobilizationofbetaglycosidasebglxfromescherichiacolionchitosangelbeads
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