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: | Conference or Workshop Item |
| Language: | English |
| Published: |
Kulliyah of Engineering, International Islamic University Malaysia
2016
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| Subjects: | |
| Online Access: | http://irep.iium.edu.my/51746/ http://irep.iium.edu.my/51746/ http://irep.iium.edu.my/51746/1/51746.pdf |
| Summary: | 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. |
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