Abstract |
Cicer α- galactosidase was immobilized onto functionalized graphene with immobilization efficiency of 84% using response surface methodology (Box-Behnken design). The immobilized enzyme had higher thermal stability than the soluble one, attractive for industrial applications. Immobilization of the enzyme lowered the Km to 1/3rd compared to the soluble enzyme. Raffinose family oligosaccharides (RFOs) are mainly responsible for flatulence by taking soybean derived food products. The immobilized enzyme can be used effectively for the hydrolysis of RFOs. After ten successive runs, the immobilized enzyme still retained approximately 60% activity, with soybean RFOs. The easy availability of enzyme source, ease of its immobilization on matrices, non-toxicity, increased stability of immobilized enzyme and effective hydrolysis of RFOs increase the Cicer α- galactosidase application in food processing industries.
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Authors | Neelesh Singh, Garima Srivastava, Mahe Talat, Himanshu Raghubanshi, Onkar Nath Srivastava, Arvind M Kayastha |
Journal | Food chemistry
(Food Chem)
Vol. 142
Pg. 430-8
(Jan 01 2014)
ISSN: 1873-7072 [Electronic] England |
PMID | 24001862
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright © 2013 Elsevier Ltd. All rights reserved. |
Chemical References |
- Enzymes, Immobilized
- Oligosaccharides
- Plant Proteins
- Graphite
- alpha-Galactosidase
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Topics |
- Cicer
(enzymology)
- Enzyme Stability
- Enzymes, Immobilized
(chemistry)
- Graphite
(chemistry)
- Hydrogen-Ion Concentration
- Hydrolysis
- Kinetics
- Nanostructures
(chemistry)
- Oligosaccharides
(chemistry)
- Plant Proteins
(chemistry)
- Temperature
- alpha-Galactosidase
(chemistry)
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