Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio
Cross-Linked Enzyme Aggregates (CLEA) is known as one of the best enzyme immobilization technique to date. In this study, amylase extract from Zophobas morio (supermeal worm) larvae was immobilized using acetone as the precipitant, glutaraldehyde as the cross-linker and bovine serum albumin as the...
| Main Authors: | , , |
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| Format: | Proceeding Paper |
| Language: | English |
| Published: |
Kulliyah of Engineering, International Islamic University Malaysia
2016
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| Subjects: | |
| Online Access: | http://irep.iium.edu.my/51746/1/51746.pdf |
| _version_ | 1825649830856228864 |
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| author | Easa, Muhammad Noor Yusof, Faridah Abd Halim , Amanatuzzakiah |
| author_facet | Easa, Muhammad Noor Yusof, Faridah Abd Halim , Amanatuzzakiah |
| author_sort | Easa, Muhammad Noor |
| collection | IIUM |
| description | Cross-Linked Enzyme Aggregates (CLEA) is known as one of the best enzyme immobilization technique to
date. In this study, amylase extract from Zophobas morio (supermeal worm) larvae was immobilized using
acetone as the precipitant, glutaraldehyde as the cross-linker and bovine serum albumin as the additive. The
characteristics of the produced CLEA was compared to its’ soluble counterpart, in terms of pH and
temperature optimum and stabilities. The results showed that CLEA and free amylase had optimum
temperature at 55°C and 45°C, respectively. CLEA-amylase displayed greater stability against high
temperature as compared to free enzyme which has lost most of its activity when the temperature was set
beyond 45°C. At 65°C, CLEA-amylase still retained 73.2% of its activity. Results also showed that, CLEAamylase
exhibited pH optimum at 11, while it is 7 for free enzyme. Similarly, CLEA-amylase more stable
than the free form, over a wider range of pH, particularly at higher pH of 9, 10 and 11. Recyclability study
showed that CLEA-amylase can retain 14.9% of its residual activity after 6 times of repeated uses. Since it is
reusable, future works might include the evaluations of using CLEA-amylase at industrial level, remarkably
in detergent applications. |
| first_indexed | 2024-03-05T23:53:24Z |
| format | Proceeding Paper |
| id | oai:generic.eprints.org:51746 |
| institution | International Islamic University Malaysia |
| language | English |
| last_indexed | 2024-03-05T23:53:24Z |
| publishDate | 2016 |
| publisher | Kulliyah of Engineering, International Islamic University Malaysia |
| record_format | dspace |
| spelling | oai:generic.eprints.org:517462016-08-22T06:31:53Z http://irep.iium.edu.my/51746/ Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio Easa, Muhammad Noor Yusof, Faridah Abd Halim , Amanatuzzakiah QP Physiology TP248.13 Biotechnology Cross-Linked Enzyme Aggregates (CLEA) is known as one of the best enzyme immobilization technique to date. In this study, amylase extract from Zophobas morio (supermeal worm) larvae was immobilized using acetone as the precipitant, glutaraldehyde as the cross-linker and bovine serum albumin as the additive. The characteristics of the produced CLEA was compared to its’ soluble counterpart, in terms of pH and temperature optimum and stabilities. The results showed that CLEA and free amylase had optimum temperature at 55°C and 45°C, respectively. CLEA-amylase displayed greater stability against high temperature as compared to free enzyme which has lost most of its activity when the temperature was set beyond 45°C. At 65°C, CLEA-amylase still retained 73.2% of its activity. Results also showed that, CLEAamylase exhibited pH optimum at 11, while it is 7 for free enzyme. Similarly, CLEA-amylase more stable than the free form, over a wider range of pH, particularly at higher pH of 9, 10 and 11. Recyclability study showed that CLEA-amylase can retain 14.9% of its residual activity after 6 times of repeated uses. Since it is reusable, future works might include the evaluations of using CLEA-amylase at industrial level, remarkably in detergent applications. Kulliyah of Engineering, International Islamic University Malaysia 2016 Proceeding Paper PeerReviewed application/pdf en http://irep.iium.edu.my/51746/1/51746.pdf Easa, Muhammad Noor and Yusof, Faridah and Abd Halim , Amanatuzzakiah (2016) Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio. In: 4th International Conference on Biotechnology Engineering 2016 (ICBioE 2016), 25th-27th July 2016, Kuala Lumpur. http://www.iium.edu.my/icbioe/2016/ |
| spellingShingle | QP Physiology TP248.13 Biotechnology Easa, Muhammad Noor Yusof, Faridah Abd Halim , Amanatuzzakiah Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio |
| title | Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio |
| title_full | Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio |
| title_fullStr | Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio |
| title_full_unstemmed | Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio |
| title_short | Characterization of cross-linked enzyme aggregates (CLEA)-amylase from Zophobas morio |
| title_sort | characterization of cross linked enzyme aggregates clea amylase from zophobas morio |
| topic | QP Physiology TP248.13 Biotechnology |
| url | http://irep.iium.edu.my/51746/1/51746.pdf |
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