Cloning, characterization and saccharification analysis of GH12 e | 31245
Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

+44 1223 790975

Cloning, characterization and saccharification analysis of GH12 endo-1, 4-β-glucanase from Thermotoga petrophila in a mesophilic host

6th International Conference & Expo on Proteomics

March 29-31, 2016 Atlanta, USA

Fatima Akram and Ikramul Haq

Government College University, Pakistan

Posters & Accepted Abstracts: J Proteomics Bioinform

Abstract :

Production of bioethanol has received much attention in recent years and many countries have made large investments in infrastructure, process development and production facilities. Energy crisis are the leading economic constrains in developed as well as in developing countries. With the exhaustion of non-renewable resources at an exponential rate, the need to develop alternative renewable sources which can be both cost effective, environmental friendly and high in yield is the need of time. Recently, the increasing demand of energy has strongly stimulated the research on conversion of lignocellulosic plant biomass by the action of cellulases enzymes into reducing sugars for the subsequent production of bioethanol. Endoglucanases are mainly responsible for hydrolyzing the internal glycosidic bond to decrease the length of the cellulose chains. Obtaining efficient and Thermostable Endoglucanase has become the goal of much research worldwide. Therefore, our research work was focus to search for new resources of Endoglucanase which was thermostable and with high catalytic efficiency. The article focuses on the thermo-tolerant endo-1,4- �?²-glucanasegene of Thermotoga petrophila RKU-1 was cloned and over-expressed in E. coli strain BL21 CodonPlus for its potential usage for the hydrolysis of lignocellulosic biomass and in different industrial applications. Thermostable endoglucanase can be used simultaneously and directly in the saccharification procedure without a pre-cooling process of biomass. Purified enzyme was optimally active with 530 Umg-1 of specific activity against CMC at pH 6.0 and 95 �?°C which has exhibited a half- life (t1/2) of 6.6 min even at temperature as high as 97 �?°C and stable up to 8 hours at 80 �?°C. The recombinant enzyme saccharified pre-treated wheat straw and baggase to 3.32% and 3.2%, respectively after 6 hours incubation at 85 �?°C. Its thermostability, resistance to heavy metal ions and high specific activity make endoglucanase a potential and promising candidate for various industrial applications such as in textile industry (Biostoning and Biofinishing) in animal feed production, in processing of beer and fruit juice, in biomass hydrolysis (bioethanol production) and in plant oil, detergent, pulp and paper industry.

Biography :