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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| Format: | Conference or Workshop Item |
| Language: | en |
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2014
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| Online Access: | http://umpir.ump.edu.my/id/eprint/7264/1/fkksa-2014-shalyda-Immobilization_Strategy.pdf http://umpir.ump.edu.my/id/eprint/7264/ |
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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. |
| building | UMPSA Library |
| collection | Institutional Repository |
| content_provider | Universiti Malaysia Pahang Al-Sultan Abdullah |
| content_source | UMPSA Institutional Repository |
| continent | Asia |
| country | Malaysia |
| 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. |
| format | Conference or Workshop Item |
| id | my.ump.umpir.7264 |
| institution | Universiti Malaysia Pahang |
| language | en |
| publishDate | 2014 |
| record_format | eprints |
| spelling | my.ump.umpir.72642015-03-03T09:35:03Z 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. . (Published) |
| 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 http://umpir.ump.edu.my/id/eprint/7264/ |
| url_provider | http://umpir.ump.edu.my/ |