Fagbohoun Jean Bedel, Ahi Amedée Pascal, Karamoko Yahaya, Dabonné Soumaila, Kouadio Eugène Jean Parfait and Kouamé Lucien Patrice
Laboratoire de Biocatalyse et des Bioprocédés de l’Université d’Abobo-Adjamé (Abidjan, Côte d’Ivoire), 02 BP 801 Abidjan 02, Côte d’Ivoire
Key words: Bifunctional enzyme, carboxymethylcellulase, endo-beta-D-glycosidase.
Abstract
This study highlights an endo-beta-D-glycosidase from little soldier of Macrotermes subhyalinus purified by anion exchange, cation exchange and hydrophobic interaction chromatography. The only substrates that were hydrolyzed by the purified enzyme were xylans and carboxyméthylcellulose. The enzyme showed a single protein band and its relative molecular weight was estimated to be 215.45±5.63 kDa. The specific activities towards carboxymethylcellulose and xylan from Birchwood were respectively 9.32±3.78 and 8.59±2.54 U/ mg of protein. The purified enzyme showed an optimum pH of 4.6 for cellulase activity an 5.0 for xylanase activity in acetate buffer. The optimum temperature of the enzyme with CMC and xylan from Birchwood hydrolysis were found to be 60 and 55 °C respectively.
Get the original articles in Source: Volume 2, Number 2, February 2012 – IJB
Published By: International Journal of Biosciences (IJB)
Related Post: Nutritive composition and mycoflora of sundried millet seeds (Panicum miliacieum) during storage
Related Post: A critical assessment of quality status of selected sachet water in Calabar Municipality, Nigeria
