A comparative study of the effectiveness of ca-alginate and k-carrageenan beads as support material for enzyme immobilization
This research aimed to compare the effectiveness of Ca-alginate and K-carrageenan as support matrix for enzyme immobilization, especially with respect to having good retention of immobilized enzyme activity, multiple reusability and having superior maximum rate of reaction as well as ease of immobi...
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iium-483692018-04-27T06:37:21Z http://irep.iium.edu.my/48369/ A comparative study of the effectiveness of ca-alginate and k-carrageenan beads as support material for enzyme immobilization Razizad, Anis Nadzirah Jameel, Ahmad Tariq TP155 Chemical engineering This research aimed to compare the effectiveness of Ca-alginate and K-carrageenan as support matrix for enzyme immobilization, especially with respect to having good retention of immobilized enzyme activity, multiple reusability and having superior maximum rate of reaction as well as ease of immobilization. Entrapment method was employed for the immobilization of beta-glucosidase enzyme in Ca-alginate and Kcarrageenan beads. The results were compared with those of free enzyme. This study aimed to fulfill three objectives: (1) to investigate the effect of design parameters on enzyme activity; (2) to determine the reusability of immobilized catalyst, and; (3) to evaluate the kinetic parameters of beta glucosidase immobilized on calcium alginate and potassium carrageenan beads. At a fixed substrate concentration, optimum pH and bead size for enzyme immobilization on Ca-alginate were 5 and 5 mm respectively, while for the K-carrageenan these were pH 4 and 5 mm bead size. The immobilized enzyme on Ca-alginate and K-carrageenan were found to follow Michaelis-Menten kinetics. Michaelis parameters Vmax and KM for Ca-alginate were found to be 65.36 mmol/min and 8.60 mM respectively, and for K-carrageenan 61.73 mmol/min and 0.94 mM respectively, while Michaelis constants for the free enzyme were 70.42 mmol/min and 2.71 mM. Higher Vmax value for free enzyme is due to the negligible mass transfer resistance to substrate diffusion to the enzyme active sites. For the residual activity after multiple uses, Ca-alginate retained the highest activity with 60.5 % of the initial activity and K-carrageenan retained only 6.83 %. K-carrageenan seems to have high affinity for the substrate while Ca-alginate has excellent stability. Keywords���-glucosidase; K-carrageenan; Ca-alginate; Enzyme activity; Immobilization 2015-11-15 Conference or Workshop Item NonPeerReviewed application/pdf en http://irep.iium.edu.my/48369/1/ACB2015.pdf application/pdf en http://irep.iium.edu.my/48369/4/48396_A%20comparative%20study%20of%20the%20effectiveness%20of%20ca-alginate_complete.pdf Razizad, Anis Nadzirah and Jameel, Ahmad Tariq (2015) A comparative study of the effectiveness of ca-alginate and k-carrageenan beads as support material for enzyme immobilization. In: Asian Congress on Biotechnology 2015: Biotechnology and Bioeconomy for Sustainable Future, 15-19 November 2015, Istana Hotel, Kuala Lumpur, Malaysia. (Unpublished) |
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TP155 Chemical engineering Razizad, Anis Nadzirah Jameel, Ahmad Tariq A comparative study of the effectiveness of ca-alginate and k-carrageenan beads as support material for enzyme immobilization |
description |
This research aimed to compare the effectiveness of Ca-alginate and K-carrageenan as support matrix for enzyme immobilization, especially with respect to having good
retention of immobilized enzyme activity, multiple reusability and having superior maximum rate of reaction as well as ease of immobilization. Entrapment method was
employed for the immobilization of beta-glucosidase enzyme in Ca-alginate and Kcarrageenan beads. The results were compared with those of free enzyme. This study
aimed to fulfill three objectives: (1) to investigate the effect of design parameters on enzyme activity; (2) to determine the reusability of immobilized catalyst, and; (3) to evaluate the kinetic parameters of beta glucosidase immobilized on calcium alginate and potassium carrageenan beads. At a fixed substrate concentration, optimum pH and bead size for enzyme immobilization on Ca-alginate were 5 and 5 mm respectively, while for the K-carrageenan these were pH 4 and 5 mm bead size. The immobilized enzyme on Ca-alginate and K-carrageenan were found to follow Michaelis-Menten kinetics. Michaelis parameters Vmax and KM for Ca-alginate were found to be 65.36 mmol/min and 8.60 mM respectively, and for K-carrageenan 61.73 mmol/min and 0.94 mM respectively, while Michaelis constants for the free enzyme were 70.42 mmol/min and 2.71 mM. Higher Vmax value for free enzyme is due to the negligible mass transfer resistance to substrate diffusion to the enzyme active sites. For the residual activity after multiple uses, Ca-alginate retained the highest activity with 60.5 % of the initial
activity and K-carrageenan retained only 6.83 %. K-carrageenan seems to have high affinity for the substrate while Ca-alginate has excellent stability.
Keywords���-glucosidase; K-carrageenan; Ca-alginate; Enzyme activity; Immobilization |
format |
Conference or Workshop Item |
author |
Razizad, Anis Nadzirah Jameel, Ahmad Tariq |
author_facet |
Razizad, Anis Nadzirah Jameel, Ahmad Tariq |
author_sort |
Razizad, Anis Nadzirah |
title |
A comparative study of the effectiveness of ca-alginate and k-carrageenan beads as support material for enzyme immobilization |
title_short |
A comparative study of the effectiveness of ca-alginate and k-carrageenan beads as support material for enzyme immobilization |
title_full |
A comparative study of the effectiveness of ca-alginate and k-carrageenan beads as support material for enzyme immobilization |
title_fullStr |
A comparative study of the effectiveness of ca-alginate and k-carrageenan beads as support material for enzyme immobilization |
title_full_unstemmed |
A comparative study of the effectiveness of ca-alginate and k-carrageenan beads as support material for enzyme immobilization |
title_sort |
comparative study of the effectiveness of ca-alginate and k-carrageenan beads as support material for enzyme immobilization |
publishDate |
2015 |
url |
http://irep.iium.edu.my/48369/ http://irep.iium.edu.my/48369/1/ACB2015.pdf http://irep.iium.edu.my/48369/4/48396_A%20comparative%20study%20of%20the%20effectiveness%20of%20ca-alginate_complete.pdf |
first_indexed |
2023-09-18T21:08:37Z |
last_indexed |
2023-09-18T21:08:37Z |
_version_ |
1777411102186930176 |