University Links: Home Page | Site Map
Covenant University Repository

Partial Purification and Characterization of Cellulase from the Haemolymph of the African Giant Land Snail (Archachatina marginata)

Omotosho, O. E. and Omonhinmin, Conrad A. and Rotimi, Solomon and Iweala, E. E. J. and Rotimi, Oluwakemi A and Femi, Ayoade (2015) Partial Purification and Characterization of Cellulase from the Haemolymph of the African Giant Land Snail (Archachatina marginata). Biotechmology, 14 (5). pp. 248-253. ISSN 1682-296X

[img] PDF
Download (90Kb)

Abstract

The aim of this study is to partially purify and characterize the cellulase extracted from the snail haemolymph of the African giant land snail of the species, Archachatina marginata. The protein concentration of the haemolymph was found to be 168 mg mLG1 and the specific activity of the crude cellulase was found to be 0.007 U mgG1 protein using Carboxymethyl-cellulose (CMC) as the substrate. The partial purification on Sephadex G-200 produced two activity peaks. The molecular weights of the two cellulase fractions were estimated to be 112,202 and 67,000. The Michealis Menten constant (km) for cellulase was 4.3 and 2.8 mg mLG1 for the higher and lower molecular weight fractions, respectively. The multiplicity of cellulase complexes indicated that the haemolymph of A. marginata may convert derived cellulose in foodstuffs such as garlic, mushrooms and domestic wastes into sources of fuel. It is suggested that the enzyme can be used to produce value-added products, such as ethanol, citric acid, amino acids and vitamins including primary metabolites from cellulosic wastes.

Item Type: Article
Uncontrolled Keywords: Hydrolyzing enzyme, cellulosic wastes, haemolymph, gel electrophoresis, cellulase
Subjects: Q Science > Q Science (General)
Q Science > QD Chemistry
Divisions: Faculty of Engineering, Science and Mathematics > School of Chemistry
Depositing User: Mrs. Julie Ilogho
Date Deposited: 16 Sep 2018 17:05
Last Modified: 10 Mar 2020 13:22
URI: http://eprints.covenantuniversity.edu.ng/id/eprint/11625

Actions (login required)

View Item View Item