IIUM Repository

Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA)

Mahmod, Safa Senan and Yusof, Faridah and Jami, Mohammed Saedi and Khanahmadi, Soofia (2015) Development of an immobilized biocatalyst with lipase and protease activities as a multipurpose cross-linked enzyme aggregate (multi-CLEA). Process Biochemistry, 50 (12). pp. 2144-2157. ISSN 1359-5113

[img] PDF - Published Version
Restricted to Repository staff only

Download (3MB) | Request a copy

Abstract

This study focused on the production of a novel multi-CLEA comprising the enzyme activities of lipase and protease from fish viscera. A multi-CLEA is a single biocatalyst that can catalyze separate unrelated reactions, but these reactions can be conducted in one application. Tests pertaining to the effect of various additives on the multi-CLEA’s activity were performed. Response Surface Methodology’s Face Centered Central Composite Design (FCCCD) was employed to optimize the preparation parameters of the multi-CLEA in an aqueous medium. It was found that 55% (w/v) of ammonium sulfate, 65 mM of glutaraldehyde, and 0.113 mM of bovine serum albumin were the optimum levels of additives to prepare the multi-CLEA with the protease and lipase recovery activity of 43.82% and 99.91%, respectively. Multi-CLEAs were found to retain an average of more than 34% of the initial activity after five consecutive batches for both enzymes. Finally, the multi-CLEA was utilized to catalyze two reactions: improved washing process and biodiesel production. The stain removal percentage of a commercial detergent was improved by 67.78% after adding multi-CLEA. In addition, the multi-CLEA catalyzed biodiesel production from vegetable oil with a percentage conversion of 51.7%. Such results demonstrated that the multi-CLEA is a promising catalyst for biotechnological applications.

Item Type: Article (Journal)
Additional Information: 4734/48266
Uncontrolled Keywords: Multi-CLEA; Protease; Lipase; Aqueous medium; Immobilized biocatalyst; Response surface Methodology; Fish viscera
Subjects: Q Science > Q Science (General)
T Technology > TP Chemical technology > TP248.13 Biotechnology
Kulliyyahs/Centres/Divisions/Institutes (Can select more than one option. Press CONTROL button): Kulliyyah of Engineering > Department of Biotechnology Engineering
Depositing User: DR FARIDAH YUSOF
Date Deposited: 16 Feb 2016 14:57
Last Modified: 17 Jul 2016 16:43
URI: http://irep.iium.edu.my/id/eprint/48226

Actions (login required)

View Item View Item

Downloads

Downloads per month over past year