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Enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis

The peculiarity of spatially restricted diffusion and molecular collision processes results in considerable contrast in a reaction between the reactant and catalyst in the heterogeneous system from its corresponding homogeneous structure. The identification of the enzymatic hydrolysis process of pre...

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Main Authors: Wan Azelee, Nur Izyan, Nordin, Norhafiza, Md. Illias, Rosli, Abdul Manas, Nor Hasmaliana, Md. Ghazali, Mohd. Nazlee Faisal
Format: Article
Language:English
Published: Universiti Putra Malaysia Press 2020
Subjects:
TP Chemical technology
Online Access:http://eprints.utm.my/id/eprint/91732/1/NurIzyanWanAzelee2020_EnzymeKineticsStudyForHeterogeneousSystem.pdf
http://eprints.utm.my/id/eprint/91732/
http://dx.doi.org/10.47836/pjst.28.S2.16
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spelling my.utm.917322021-07-28T08:42:14Z http://eprints.utm.my/id/eprint/91732/ Enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis Wan Azelee, Nur Izyan Nordin, Norhafiza Md. Illias, Rosli Abdul Manas, Nor Hasmaliana Md. Ghazali, Mohd. Nazlee Faisal TP Chemical technology The peculiarity of spatially restricted diffusion and molecular collision processes results in considerable contrast in a reaction between the reactant and catalyst in the heterogeneous system from its corresponding homogeneous structure. The identification of the enzymatic hydrolysis process of pre-treated kenaf and to convert it into simple sugars employing a systematic kinetic investigation is the aims of this study. The influence of substrate concentration on xylanase hydrolysis was performed in water bath shakers. In-house recombinant xylanase expressed in Pichia pastoris was used for the hydrolysis at pH 4.0 in 50 mM sodium citrate buffer with 200 rpm agitation. Modified Prout-Tompkins equation was used for the heterogeneous substrate hydrolysis. The results obtained show that temperature simultaneously influenced the time dependency of the reducing sugar yield. Dependence of the enzymatic rate of reaction can be calculated effectively on the conversion of substrates over different temperatures. The activation energy needed for pretreated kenaf hydrolysis was among the least compared to other lignocelluloses, which was only 25.15 kJ/mol. In conclusion, the exponential kinetic equation by the Modified Prout-Tompkins equation offers a solid understanding of xylanase hydrolysis on the pretreated kenaf. Thus, the prediction of the degree of hydrolysis required at the predetermined temperature and time values used can be quickly and precisely determined. Universiti Putra Malaysia Press 2020 Article PeerReviewed application/pdf en http://eprints.utm.my/id/eprint/91732/1/NurIzyanWanAzelee2020_EnzymeKineticsStudyForHeterogeneousSystem.pdf Wan Azelee, Nur Izyan and Nordin, Norhafiza and Md. Illias, Rosli and Abdul Manas, Nor Hasmaliana and Md. Ghazali, Mohd. Nazlee Faisal (2020) Enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis. Pertanika Journal of Science and Technology, 28 (SI2). pp. 197-216. ISSN 0128-7680 http://dx.doi.org/10.47836/pjst.28.S2.16
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
language English
topic TP Chemical technology
spellingShingle TP Chemical technology
Wan Azelee, Nur Izyan
Nordin, Norhafiza
Md. Illias, Rosli
Abdul Manas, Nor Hasmaliana
Md. Ghazali, Mohd. Nazlee Faisal
Enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis
description The peculiarity of spatially restricted diffusion and molecular collision processes results in considerable contrast in a reaction between the reactant and catalyst in the heterogeneous system from its corresponding homogeneous structure. The identification of the enzymatic hydrolysis process of pre-treated kenaf and to convert it into simple sugars employing a systematic kinetic investigation is the aims of this study. The influence of substrate concentration on xylanase hydrolysis was performed in water bath shakers. In-house recombinant xylanase expressed in Pichia pastoris was used for the hydrolysis at pH 4.0 in 50 mM sodium citrate buffer with 200 rpm agitation. Modified Prout-Tompkins equation was used for the heterogeneous substrate hydrolysis. The results obtained show that temperature simultaneously influenced the time dependency of the reducing sugar yield. Dependence of the enzymatic rate of reaction can be calculated effectively on the conversion of substrates over different temperatures. The activation energy needed for pretreated kenaf hydrolysis was among the least compared to other lignocelluloses, which was only 25.15 kJ/mol. In conclusion, the exponential kinetic equation by the Modified Prout-Tompkins equation offers a solid understanding of xylanase hydrolysis on the pretreated kenaf. Thus, the prediction of the degree of hydrolysis required at the predetermined temperature and time values used can be quickly and precisely determined.
format Article
author Wan Azelee, Nur Izyan
Nordin, Norhafiza
Md. Illias, Rosli
Abdul Manas, Nor Hasmaliana
Md. Ghazali, Mohd. Nazlee Faisal
author_facet Wan Azelee, Nur Izyan
Nordin, Norhafiza
Md. Illias, Rosli
Abdul Manas, Nor Hasmaliana
Md. Ghazali, Mohd. Nazlee Faisal
author_sort Wan Azelee, Nur Izyan
title Enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis
title_short Enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis
title_full Enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis
title_fullStr Enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis
title_full_unstemmed Enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis
title_sort enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis
publisher Universiti Putra Malaysia Press
publishDate 2020
url http://eprints.utm.my/id/eprint/91732/1/NurIzyanWanAzelee2020_EnzymeKineticsStudyForHeterogeneousSystem.pdf
http://eprints.utm.my/id/eprint/91732/
http://dx.doi.org/10.47836/pjst.28.S2.16
_version_ 1706956986433667072
score 13.211869

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