Immobilization Strategy of Recombinant Xylanase from Trichoderma reesei by Cross-linked Enzyme Aggregates

Abstract—Modern developments in biotechnology have paved the way for extensive use of biocatalysis in industries. Although offering immense potential, industrial application is usually hampered by lack of operational stability, difficulty in recovery as well as limited re-use of the enzyme. These dr...

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Main Authors: Md Shaarani, S., Md Jahim, J., A. Rahman, R., Md Illias, R.
Format: Conference or Workshop Item
Language:English
Published: 2014
Subjects:
Online Access:http://umpir.ump.edu.my/id/eprint/7264/1/fkksa-2014-shalyda-Immobilization_Strategy.pdf
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author Md Shaarani, S.
Md Jahim, J.
A. Rahman, R.
Md Illias, R.
author_facet Md Shaarani, S.
Md Jahim, J.
A. Rahman, R.
Md Illias, R.
author_sort Md Shaarani, S.
collection UMP
description Abstract—Modern developments in biotechnology have paved the way for extensive use of biocatalysis in industries. Although offering immense potential, industrial application is usually hampered by lack of operational stability, difficulty in recovery as well as limited re-use of the enzyme. These drawbacks however can be overcome by immobilization. Cross-linked enzyme aggregates (CLEAs), a versatile carrier-free immobilization technique is one that is currently capturing global interest. This approach involves precipitating soluble enzyme with an appropriate precipitant and subsequent crosslinking by a crosslinking reagent. Without ineffective carriers, CLEAs offer high enzymatic activity, stability and reduced production cost. This study demonstrated successful CLEA synthesis of recombinant xylanase from Trichoderma reesei using ethanol as aggregating agent and glutaraldehyde (2% (v/v); 100 mM) as crosslinker. Effects of additives including proteic feeder such as bovine serum albumin (BSA) and poly-L-Lysine were investigated to reveal its significance in enhancing the performance of enzyme. Addition of 0.1 mg BSA/U xylanase showed considerable increment in CLEA development with approximately 50% retained activity.
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spelling UMPir72642015-03-03T09:35:03Z http://umpir.ump.edu.my/id/eprint/7264/ Immobilization Strategy of Recombinant Xylanase from Trichoderma reesei by Cross-linked Enzyme Aggregates Md Shaarani, S. Md Jahim, J. A. Rahman, R. Md Illias, R. TP Chemical technology Abstract—Modern developments in biotechnology have paved the way for extensive use of biocatalysis in industries. Although offering immense potential, industrial application is usually hampered by lack of operational stability, difficulty in recovery as well as limited re-use of the enzyme. These drawbacks however can be overcome by immobilization. Cross-linked enzyme aggregates (CLEAs), a versatile carrier-free immobilization technique is one that is currently capturing global interest. This approach involves precipitating soluble enzyme with an appropriate precipitant and subsequent crosslinking by a crosslinking reagent. Without ineffective carriers, CLEAs offer high enzymatic activity, stability and reduced production cost. This study demonstrated successful CLEA synthesis of recombinant xylanase from Trichoderma reesei using ethanol as aggregating agent and glutaraldehyde (2% (v/v); 100 mM) as crosslinker. Effects of additives including proteic feeder such as bovine serum albumin (BSA) and poly-L-Lysine were investigated to reveal its significance in enhancing the performance of enzyme. Addition of 0.1 mg BSA/U xylanase showed considerable increment in CLEA development with approximately 50% retained activity. 2014 Conference or Workshop Item NonPeerReviewed application/pdf en http://umpir.ump.edu.my/id/eprint/7264/1/fkksa-2014-shalyda-Immobilization_Strategy.pdf Md Shaarani, S. and Md Jahim, J. and A. Rahman, R. and Md Illias, R. (2014) Immobilization Strategy of Recombinant Xylanase from Trichoderma reesei by Cross-linked Enzyme Aggregates. In: International Conference on Bioengineering (ICBE 2014) , 19-20 June 2014 , Venice, Italy. .
spellingShingle TP Chemical technology
Md Shaarani, S.
Md Jahim, J.
A. Rahman, R.
Md Illias, R.
Immobilization Strategy of Recombinant Xylanase from Trichoderma reesei by Cross-linked Enzyme Aggregates
title Immobilization Strategy of Recombinant Xylanase from Trichoderma reesei by Cross-linked Enzyme Aggregates
title_full Immobilization Strategy of Recombinant Xylanase from Trichoderma reesei by Cross-linked Enzyme Aggregates
title_fullStr Immobilization Strategy of Recombinant Xylanase from Trichoderma reesei by Cross-linked Enzyme Aggregates
title_full_unstemmed Immobilization Strategy of Recombinant Xylanase from Trichoderma reesei by Cross-linked Enzyme Aggregates
title_short Immobilization Strategy of Recombinant Xylanase from Trichoderma reesei by Cross-linked Enzyme Aggregates
title_sort immobilization strategy of recombinant xylanase from trichoderma reesei by cross linked enzyme aggregates
topic TP Chemical technology
url http://umpir.ump.edu.my/id/eprint/7264/1/fkksa-2014-shalyda-Immobilization_Strategy.pdf
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