Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei

Numerous state-of-the-art technologies and new types of carriers have been developed recently to improve enzyme immobilization. Cross-linked enzyme aggregate (CLEA) technology is a lucrative prospect, as several robust biocatalysts have been generated using this simple method of carrier-free immobil...

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Main Authors:	Shalyda, Md Shaarani, Jamaliah, Md Jahim, Roshanida, A. Rahman, Ani, Idris, Abdul Munir, Abdul Murad, Rosli, Md. Illias
Format:	Article
Language:	English
Published:	Elsevier Ltd 2016
Subjects:	TP Chemical technology
Online Access:	http://umpir.ump.edu.my/id/eprint/13894/ http://umpir.ump.edu.my/id/eprint/13894/ http://umpir.ump.edu.my/id/eprint/13894/ http://umpir.ump.edu.my/id/eprint/13894/1/Silanized%20Maghemite%20for%20Cross-linked%20Enzyme%20Aggregates%20of%20Recombinant%20Xylanase%20from%20Trichoderma%20reesei.pdf

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spelling	ump-138942018-02-05T01:24:13Z http://umpir.ump.edu.my/id/eprint/13894/ Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei Shalyda, Md Shaarani Jamaliah, Md Jahim Roshanida, A. Rahman Ani, Idris Abdul Munir, Abdul Murad Rosli, Md. Illias TP Chemical technology Numerous state-of-the-art technologies and new types of carriers have been developed recently to improve enzyme immobilization. Cross-linked enzyme aggregate (CLEA) technology is a lucrative prospect, as several robust biocatalysts have been generated using this simple method of carrier-free immobilization with the possibility of using semipurified enzyme. However, the low lysine content in the enzyme remains a challenge for effective crosslinking. In this work, maghemite (γ- Fe2O3), a recently sought after nanoparticle, was silanized with (3-aminopropyl) triethoxysilane (APTES) for use in the preparation of cross-linked enzyme aggregates of recombinant xylanase from Trichoderma reesei (Xyl-CLEA-silanized maghemite). Prior screening revealed ethanol to be the best precipitant, and a 0.2: 1 (v:v) glutaraldehyde to enzyme ratio was essential to form active CLEAs. The Xyl-CLEA-silanized maghemite succeeded in increasing the activity recovery 1.66- and 1.5-fold compared to conventional Xyl-CLEAs and Xyl-CLEA-BSA, respectively. The silanization of maghemite with APTES was proven feasible when a 0.0075:1 (v:v) maghemite to enzyme ratio was able to achieve a 78% activity recovery of the xylanase aggregates, whereas the non-silanized maghemite only achieved a 47% activity recovery. At an elevated temperature of 60 °C, Xyl-CLEA-silanized maghemite retained approximately 50% of its initial activity, compared to the free enzyme, for which the activity recovery had plummeted to 20%. Conversely, Xyl-CLEA suffered a total loss of activity at this temperature, whereas Xyl-CLEA-BSA retained only a 6% activity. Xyl-CLEA-silanized maghemite also successfully retained more than 50% of its activity after up to 6 cycles, whereas Xyl-CLEA retained approximately 10% of its initial activity after only 5 cycles. The surface morphology, particle size and loading of silanized maghemite were confirmed by field emission scanning electron microscopy (FESEM) and Fourier transform infrared (FTIR) spectroscopy. The combination of the effective surface modification, high enzyme activity recovery, improved stability and enhanced reusability of Xyl-CLEA-silanized maghemite presents an attractive process for xylanase immobilization and provides a promising catalyst for the biomass industry. Elsevier Ltd 2016 Article PeerReviewed application/pdf en http://umpir.ump.edu.my/id/eprint/13894/1/Silanized%20Maghemite%20for%20Cross-linked%20Enzyme%20Aggregates%20of%20Recombinant%20Xylanase%20from%20Trichoderma%20reesei.pdf Shalyda, Md Shaarani and Jamaliah, Md Jahim and Roshanida, A. Rahman and Ani, Idris and Abdul Munir, Abdul Murad and Rosli, Md. Illias (2016) Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei. Journal of Molecular Catalysis B: Enzymatic, 133. pp. 65-76. ISSN 1381-1177 http://dx.doi.org/10.1016/j.molcatb.2016.07.006 DOI: 10.1016/j.molcatb.2016.07.006
repository_type	Digital Repository
institution_category	Local University
institution	Universiti Malaysia Pahang
building	UMP Institutional Repository
collection	Online Access
language	English
topic	TP Chemical technology
spellingShingle	TP Chemical technology Shalyda, Md Shaarani Jamaliah, Md Jahim Roshanida, A. Rahman Ani, Idris Abdul Munir, Abdul Murad Rosli, Md. Illias Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei
description	Numerous state-of-the-art technologies and new types of carriers have been developed recently to improve enzyme immobilization. Cross-linked enzyme aggregate (CLEA) technology is a lucrative prospect, as several robust biocatalysts have been generated using this simple method of carrier-free immobilization with the possibility of using semipurified enzyme. However, the low lysine content in the enzyme remains a challenge for effective crosslinking. In this work, maghemite (γ- Fe2O3), a recently sought after nanoparticle, was silanized with (3-aminopropyl) triethoxysilane (APTES) for use in the preparation of cross-linked enzyme aggregates of recombinant xylanase from Trichoderma reesei (Xyl-CLEA-silanized maghemite). Prior screening revealed ethanol to be the best precipitant, and a 0.2: 1 (v:v) glutaraldehyde to enzyme ratio was essential to form active CLEAs. The Xyl-CLEA-silanized maghemite succeeded in increasing the activity recovery 1.66- and 1.5-fold compared to conventional Xyl-CLEAs and Xyl-CLEA-BSA, respectively. The silanization of maghemite with APTES was proven feasible when a 0.0075:1 (v:v) maghemite to enzyme ratio was able to achieve a 78% activity recovery of the xylanase aggregates, whereas the non-silanized maghemite only achieved a 47% activity recovery. At an elevated temperature of 60 °C, Xyl-CLEA-silanized maghemite retained approximately 50% of its initial activity, compared to the free enzyme, for which the activity recovery had plummeted to 20%. Conversely, Xyl-CLEA suffered a total loss of activity at this temperature, whereas Xyl-CLEA-BSA retained only a 6% activity. Xyl-CLEA-silanized maghemite also successfully retained more than 50% of its activity after up to 6 cycles, whereas Xyl-CLEA retained approximately 10% of its initial activity after only 5 cycles. The surface morphology, particle size and loading of silanized maghemite were confirmed by field emission scanning electron microscopy (FESEM) and Fourier transform infrared (FTIR) spectroscopy. The combination of the effective surface modification, high enzyme activity recovery, improved stability and enhanced reusability of Xyl-CLEA-silanized maghemite presents an attractive process for xylanase immobilization and provides a promising catalyst for the biomass industry.
format	Article
author	Shalyda, Md Shaarani Jamaliah, Md Jahim Roshanida, A. Rahman Ani, Idris Abdul Munir, Abdul Murad Rosli, Md. Illias
author_facet	Shalyda, Md Shaarani Jamaliah, Md Jahim Roshanida, A. Rahman Ani, Idris Abdul Munir, Abdul Murad Rosli, Md. Illias
author_sort	Shalyda, Md Shaarani
title	Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei
title_short	Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei
title_full	Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei
title_fullStr	Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei
title_full_unstemmed	Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei
title_sort	silanized maghemite for cross-linked enzyme aggregates of recombinant xylanase from trichoderma reesei
publisher	Elsevier Ltd
publishDate	2016
url	http://umpir.ump.edu.my/id/eprint/13894/ http://umpir.ump.edu.my/id/eprint/13894/ http://umpir.ump.edu.my/id/eprint/13894/ http://umpir.ump.edu.my/id/eprint/13894/1/Silanized%20Maghemite%20for%20Cross-linked%20Enzyme%20Aggregates%20of%20Recombinant%20Xylanase%20from%20Trichoderma%20reesei.pdf
first_indexed	2023-09-18T22:17:01Z
last_indexed	2023-09-18T22:17:01Z
_version_	1777415404981846016

Silanized Maghemite for Cross-linked Enzyme Aggregates of Recombinant Xylanase from Trichoderma reesei

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