Novel epoxy activated hydrogels for solving lactose intolerance

"Lactose intolerance" is a medical problem for almost 70% of the world population. Milk and dairy products contain 5-10% w/v lactose. Hydrolysis of lactose by immobilized lactase is an industrial solution. In this work, we succeeded to increase the lactase loading capacity to more than 3-f...

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Main Authors: Elnashar, Magdy, Hassan, M.
Format: Journal Article
Published: Hindawi Publishing Corporation 2014
Online Access:http://hdl.handle.net/20.500.11937/4892
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author Elnashar, Magdy
Hassan, M.
author_facet Elnashar, Magdy
Hassan, M.
author_sort Elnashar, Magdy
building Curtin Institutional Repository
collection Online Access
description "Lactose intolerance" is a medical problem for almost 70% of the world population. Milk and dairy products contain 5-10% w/v lactose. Hydrolysis of lactose by immobilized lactase is an industrial solution. In this work, we succeeded to increase the lactase loading capacity to more than 3-fold to 36.3 U/g gel using epoxy activated hydrogels compared to 11 U/g gel using aldehyde activated carrageenan. The hydrogel's mode of interaction was proven by FTIR, DSC, and TGA. The high activity of the epoxy group was regarded to its ability to attach to the enzyme's -SH, -NH, and -OH groups, whereas the aldehyde group could only bind to the enzyme's -NH2 group. The optimum conditions for immobilization such as epoxy chain length and enzyme concentration have been studied. Furthermore, the optimum enzyme conditions were also deliberated and showed better stability for the immobilized enzyme and the Michaelis constants, Km and Vmax, were doubled. Results revealed also that both free and immobilized enzymes reached their maximum rate of lactose conversion after 2 h, albeit, the aldehyde activated hydrogel could only reach 63% of the free enzyme. In brief, the epoxy activated hydrogels are more efficient in immobilizing more enzymes than the aldehyde activated hydrogel.
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spelling curtin-20.500.11937-48922017-09-13T14:45:48Z Novel epoxy activated hydrogels for solving lactose intolerance Elnashar, Magdy Hassan, M. "Lactose intolerance" is a medical problem for almost 70% of the world population. Milk and dairy products contain 5-10% w/v lactose. Hydrolysis of lactose by immobilized lactase is an industrial solution. In this work, we succeeded to increase the lactase loading capacity to more than 3-fold to 36.3 U/g gel using epoxy activated hydrogels compared to 11 U/g gel using aldehyde activated carrageenan. The hydrogel's mode of interaction was proven by FTIR, DSC, and TGA. The high activity of the epoxy group was regarded to its ability to attach to the enzyme's -SH, -NH, and -OH groups, whereas the aldehyde group could only bind to the enzyme's -NH2 group. The optimum conditions for immobilization such as epoxy chain length and enzyme concentration have been studied. Furthermore, the optimum enzyme conditions were also deliberated and showed better stability for the immobilized enzyme and the Michaelis constants, Km and Vmax, were doubled. Results revealed also that both free and immobilized enzymes reached their maximum rate of lactose conversion after 2 h, albeit, the aldehyde activated hydrogel could only reach 63% of the free enzyme. In brief, the epoxy activated hydrogels are more efficient in immobilizing more enzymes than the aldehyde activated hydrogel. 2014 Journal Article http://hdl.handle.net/20.500.11937/4892 10.1155/2014/817985 Hindawi Publishing Corporation fulltext
spellingShingle Elnashar, Magdy
Hassan, M.
Novel epoxy activated hydrogels for solving lactose intolerance
title Novel epoxy activated hydrogels for solving lactose intolerance
title_full Novel epoxy activated hydrogels for solving lactose intolerance
title_fullStr Novel epoxy activated hydrogels for solving lactose intolerance
title_full_unstemmed Novel epoxy activated hydrogels for solving lactose intolerance
title_short Novel epoxy activated hydrogels for solving lactose intolerance
title_sort novel epoxy activated hydrogels for solving lactose intolerance
url http://hdl.handle.net/20.500.11937/4892