Characterisation of recombinant Trichoderma reesei cellobiohydrolase and the potential of cellulase mixture in hydrolyzing oil palm empty fruit bunches

The potential for recombinant cellulases from fungi to hydrolyze oil palm empty fruit bunches (OPEFB) into simple sugars was investigated. A mixture of two recombinant enzymes consisting of a cellobiohydrolase from Trichoderma reesei and an endoglucanase from Aspergillus niger, was evaluated for O...

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Main Authors: Quay, Doris Huai Xia, Yong, Hui Yee, Rosli Md Illias, Nor Muhammad Mahadi, Farah Diba Abu Bakar, Abdul Munir Abdul Murad
Format: Article
Language:English
Published: Penerbit Universiti Kebangsaan Malaysia 2017
Online Access:http://journalarticle.ukm.my/12327/
http://journalarticle.ukm.my/12327/1/46_02_02.pdf
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author Quay, Doris Huai Xia
Yong, Hui Yee
Rosli Md Illias,
Nor Muhammad Mahadi,
Farah Diba Abu Bakar,
Abdul Munir Abdul Murad,
author_facet Quay, Doris Huai Xia
Yong, Hui Yee
Rosli Md Illias,
Nor Muhammad Mahadi,
Farah Diba Abu Bakar,
Abdul Munir Abdul Murad,
author_sort Quay, Doris Huai Xia
building UKM Institutional Repository
collection Online Access
description The potential for recombinant cellulases from fungi to hydrolyze oil palm empty fruit bunches (OPEFB) into simple sugars was investigated. A mixture of two recombinant enzymes consisting of a cellobiohydrolase from Trichoderma reesei and an endoglucanase from Aspergillus niger, was evaluated for OPEFB hydrolysis. The development of A. niger endoglucanase has been described previously. In this work, the development of a recombinant cellobiohydrolase and the activity of this enzyme mixture towards OPEFB hydrolysis were described. To obtain recombinant cellobiohydrolase, the cDNA encoding for cellobiohydrolase, cbhII, was isolated from the T. reesei strain M5, and the gene was expressed in the methylotrophic yeast, Pichia pastoris. Partially purified CbhII demonstrated optimum activity at 50°C and pH 5.0. This enzyme was shown to hydrolyze Avicel at a concentration of 0.486 U/mg under optimum conditions. Hydrolysis of pretreated OPEFB using CbhII and endoglucanase EglA showed that the total reducing sugar produced was higher in the enzyme mixture reaction than were produced in an individual enzyme reaction. Addition of β-glucosidase and an enzyme cofactor significantly increased enzyme activity and OPEFB cellulose hydrolysis. This study demonstrated the capability of an enzyme mixture to produce sugars from oil palm lignocellulosic waste.
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spelling oai:generic.eprints.org:123272018-11-16T21:10:58Z http://journalarticle.ukm.my/12327/ Characterisation of recombinant Trichoderma reesei cellobiohydrolase and the potential of cellulase mixture in hydrolyzing oil palm empty fruit bunches Quay, Doris Huai Xia Yong, Hui Yee Rosli Md Illias, Nor Muhammad Mahadi, Farah Diba Abu Bakar, Abdul Munir Abdul Murad, The potential for recombinant cellulases from fungi to hydrolyze oil palm empty fruit bunches (OPEFB) into simple sugars was investigated. A mixture of two recombinant enzymes consisting of a cellobiohydrolase from Trichoderma reesei and an endoglucanase from Aspergillus niger, was evaluated for OPEFB hydrolysis. The development of A. niger endoglucanase has been described previously. In this work, the development of a recombinant cellobiohydrolase and the activity of this enzyme mixture towards OPEFB hydrolysis were described. To obtain recombinant cellobiohydrolase, the cDNA encoding for cellobiohydrolase, cbhII, was isolated from the T. reesei strain M5, and the gene was expressed in the methylotrophic yeast, Pichia pastoris. Partially purified CbhII demonstrated optimum activity at 50°C and pH 5.0. This enzyme was shown to hydrolyze Avicel at a concentration of 0.486 U/mg under optimum conditions. Hydrolysis of pretreated OPEFB using CbhII and endoglucanase EglA showed that the total reducing sugar produced was higher in the enzyme mixture reaction than were produced in an individual enzyme reaction. Addition of β-glucosidase and an enzyme cofactor significantly increased enzyme activity and OPEFB cellulose hydrolysis. This study demonstrated the capability of an enzyme mixture to produce sugars from oil palm lignocellulosic waste. Penerbit Universiti Kebangsaan Malaysia 2017-06 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/12327/1/46_02_02.pdf Quay, Doris Huai Xia and Yong, Hui Yee and Rosli Md Illias, and Nor Muhammad Mahadi, and Farah Diba Abu Bakar, and Abdul Munir Abdul Murad, (2017) Characterisation of recombinant Trichoderma reesei cellobiohydrolase and the potential of cellulase mixture in hydrolyzing oil palm empty fruit bunches. Malaysian Applied Biology, 46 (2). pp. 11-19. ISSN 0126-8643 http://www.mabjournal.com/index.php?option=com_content&view=article&id=644&catid=59:current-view&Itemid=56
spellingShingle Quay, Doris Huai Xia
Yong, Hui Yee
Rosli Md Illias,
Nor Muhammad Mahadi,
Farah Diba Abu Bakar,
Abdul Munir Abdul Murad,
Characterisation of recombinant Trichoderma reesei cellobiohydrolase and the potential of cellulase mixture in hydrolyzing oil palm empty fruit bunches
title Characterisation of recombinant Trichoderma reesei cellobiohydrolase and the potential of cellulase mixture in hydrolyzing oil palm empty fruit bunches
title_full Characterisation of recombinant Trichoderma reesei cellobiohydrolase and the potential of cellulase mixture in hydrolyzing oil palm empty fruit bunches
title_fullStr Characterisation of recombinant Trichoderma reesei cellobiohydrolase and the potential of cellulase mixture in hydrolyzing oil palm empty fruit bunches
title_full_unstemmed Characterisation of recombinant Trichoderma reesei cellobiohydrolase and the potential of cellulase mixture in hydrolyzing oil palm empty fruit bunches
title_short Characterisation of recombinant Trichoderma reesei cellobiohydrolase and the potential of cellulase mixture in hydrolyzing oil palm empty fruit bunches
title_sort characterisation of recombinant trichoderma reesei cellobiohydrolase and the potential of cellulase mixture in hydrolyzing oil palm empty fruit bunches
url http://journalarticle.ukm.my/12327/
http://journalarticle.ukm.my/12327/
http://journalarticle.ukm.my/12327/1/46_02_02.pdf