Effect of xylanase immobilisation conditions by combination of entrapment and covalent binding on alginate beads
The immobilisation of enzymes offer improvement in enzyme stability and characteristics as well as overcome the limitations of free enzyme systems for commercial purposes. In the current study, xylanase was immobilised using a combination technique of entrapment and covalent binding within and onto...
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| Format: | Conference or Workshop Item |
| Language: | English |
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IOP Publishing Ltd
2020
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| Online Access: | http://umpir.ump.edu.my/id/eprint/37368/ http://umpir.ump.edu.my/id/eprint/37368/1/Effect%20of%20xylanase%20immobilisation%20conditions%20by%20combination%20of%20entrapment.pdf |
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| author | Siti Sabrina, Mohd Sukri Mimi Sakinah, Abdul Munaim Wan Zuraida, Wan Kamis H., Hassan A. K., Nur Fadzeelah Sharifah K., Jamaludin |
| author_facet | Siti Sabrina, Mohd Sukri Mimi Sakinah, Abdul Munaim Wan Zuraida, Wan Kamis H., Hassan A. K., Nur Fadzeelah Sharifah K., Jamaludin |
| author_sort | Siti Sabrina, Mohd Sukri |
| building | UMP Institutional Repository |
| collection | Online Access |
| description | The immobilisation of enzymes offer improvement in enzyme stability and characteristics as well as overcome the limitations of free enzyme systems for commercial purposes. In the current study, xylanase was immobilised using a combination technique of entrapment and covalent binding within and onto calcium alginate beads. The sodium alginate and calcium chloride (CaCl2) concentration used for the preparation of alginate beads which is the support matrix for xylanase immobilisation were fixed at 3% (w/v) and 0.3 M, respectively. The effect of immobilisation conditions (agitation rate, enzyme loading, and glutaraldehyde concentration) were studied using One-Factor-At-a-Time (OFAT) approach. The best condition for optimum immobilisation yield (83.93%) was found to be made up of the following parameter combination: agitation rate, 200 rpm; xylanase loading, 200 U; and glutaraldehyde concentration, 12% (w/w). The study shows the immobilisation conditions play a significant role towards the immobilisation yield of xylanase. |
| first_indexed | 2025-11-15T03:25:40Z |
| format | Conference or Workshop Item |
| id | ump-37368 |
| institution | Universiti Malaysia Pahang |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T03:25:40Z |
| publishDate | 2020 |
| publisher | IOP Publishing Ltd |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | ump-373682023-06-08T04:28:54Z http://umpir.ump.edu.my/id/eprint/37368/ Effect of xylanase immobilisation conditions by combination of entrapment and covalent binding on alginate beads Siti Sabrina, Mohd Sukri Mimi Sakinah, Abdul Munaim Wan Zuraida, Wan Kamis H., Hassan A. K., Nur Fadzeelah Sharifah K., Jamaludin QD Chemistry TP Chemical technology The immobilisation of enzymes offer improvement in enzyme stability and characteristics as well as overcome the limitations of free enzyme systems for commercial purposes. In the current study, xylanase was immobilised using a combination technique of entrapment and covalent binding within and onto calcium alginate beads. The sodium alginate and calcium chloride (CaCl2) concentration used for the preparation of alginate beads which is the support matrix for xylanase immobilisation were fixed at 3% (w/v) and 0.3 M, respectively. The effect of immobilisation conditions (agitation rate, enzyme loading, and glutaraldehyde concentration) were studied using One-Factor-At-a-Time (OFAT) approach. The best condition for optimum immobilisation yield (83.93%) was found to be made up of the following parameter combination: agitation rate, 200 rpm; xylanase loading, 200 U; and glutaraldehyde concentration, 12% (w/w). The study shows the immobilisation conditions play a significant role towards the immobilisation yield of xylanase. IOP Publishing Ltd 2020-07-09 Conference or Workshop Item PeerReviewed pdf en cc_by http://umpir.ump.edu.my/id/eprint/37368/1/Effect%20of%20xylanase%20immobilisation%20conditions%20by%20combination%20of%20entrapment.pdf Siti Sabrina, Mohd Sukri and Mimi Sakinah, Abdul Munaim and Wan Zuraida, Wan Kamis and H., Hassan and A. K., Nur Fadzeelah and Sharifah K., Jamaludin (2020) Effect of xylanase immobilisation conditions by combination of entrapment and covalent binding on alginate beads. In: IOP Conference Series: Materials Science and Engineering; 2nd Joint Conference on Green Engineering Technology and Applied Computing 2020, IConGETech 2020 and International Conference on Applied Computing 2020, ICAC 2020 , 4 - 5 February 2020 , Bangkok. pp. 1-7., 864 (012026). ISSN 1757-8981 (Published) https://doi.org/10.1088/1757-899X/864/1/012026 |
| spellingShingle | QD Chemistry TP Chemical technology Siti Sabrina, Mohd Sukri Mimi Sakinah, Abdul Munaim Wan Zuraida, Wan Kamis H., Hassan A. K., Nur Fadzeelah Sharifah K., Jamaludin Effect of xylanase immobilisation conditions by combination of entrapment and covalent binding on alginate beads |
| title | Effect of xylanase immobilisation conditions by combination of entrapment and covalent binding on alginate beads |
| title_full | Effect of xylanase immobilisation conditions by combination of entrapment and covalent binding on alginate beads |
| title_fullStr | Effect of xylanase immobilisation conditions by combination of entrapment and covalent binding on alginate beads |
| title_full_unstemmed | Effect of xylanase immobilisation conditions by combination of entrapment and covalent binding on alginate beads |
| title_short | Effect of xylanase immobilisation conditions by combination of entrapment and covalent binding on alginate beads |
| title_sort | effect of xylanase immobilisation conditions by combination of entrapment and covalent binding on alginate beads |
| topic | QD Chemistry TP Chemical technology |
| url | http://umpir.ump.edu.my/id/eprint/37368/ http://umpir.ump.edu.my/id/eprint/37368/ http://umpir.ump.edu.my/id/eprint/37368/1/Effect%20of%20xylanase%20immobilisation%20conditions%20by%20combination%20of%20entrapment.pdf |