IIUM Repository

Immobilization of lipase in functionalised potassium carrageenan beads and optimization of the enzyme activity

Fauzli, Farah Nabila and Jameel, Ahmad Tariq (2018) Immobilization of lipase in functionalised potassium carrageenan beads and optimization of the enzyme activity. In: 5th International Conference on Biotechnology Engineering (ICBioE 2018), 19th-20th September 2018, Kuala Lumpur.

[img] PDF - Published Version
Restricted to Registered users only

Download (959kB) | Request a copy

Abstract

Lipase enzyme is widely used as catalysis for the hydrolysis of fats and lipid to glycerol. It has gained a high demand due to its extensive application as catalyst in variety of other applications such as biosensor development, and food and pharmaceutical industries. However, soluble enzymes in industrial applications encounter difficulty in recovery, as well as the stability and reusability of the enzyme. These limitations can be largely overcome by immobilization of enzymes on suitable solid supports. This research focuses on the immobilization of lipase on the functionalized potassium-carrageenan beads and examined the optimum enzymatic activity using p-nitrophenyl palmitate as substrate. The probable mechanism for immobilization was cross-linking and covalent bonding obtained with the addition of Glutaraldehyde (GA) and Polyethyleneimine (PEI) solution during curing of potassium carrageenan beads. The beads were functionalized by treatment with Glutaraldehyde (GA) and Polyethyleneimine (PEI) prior to immobilization. The effects of enzyme concentration, curing time, temperature and pH values on the enzyme loading and enzymatic activity were studied. The maximum enzyme loading was obtained at 1 hour curing time and 50mg/mL lipase concentration. The maximum lipase activity was found at 35⁰C and pH 8.

Item Type: Conference or Workshop Item (Plenary Papers)
Additional Information: 5642/66904
Uncontrolled Keywords: lipaze enzyme; immobilization; pottasium carrageenan beads; enzyme activity; functionalization
Subjects: T Technology > TP Chemical technology > TP155 Chemical engineering
T Technology > TP Chemical technology > TP248.13 Biotechnology
Kulliyyahs/Centres/Divisions/Institutes (Can select more than one option. Press CONTROL button): Kulliyyah of Engineering
Kulliyyah of Engineering > Department of Biotechnology Engineering
Depositing User: Dr. Ahmad Tariq Jameel
Date Deposited: 17 Oct 2018 15:45
Last Modified: 15 Jan 2019 09:08
URI: http://irep.iium.edu.my/id/eprint/66904

Actions (login required)

View Item View Item

Downloads

Downloads per month over past year

Loading...