| Autor: |
Femi Kayode Agboola, Adedeji Nelson Ademakinwa, Zainab Adenike Ayinla |
| Rok vydání: |
2021 |
| Předmět: |
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| DOI: |
10.21203/rs.3.rs-783369/v1 |
| Popis: |
Aureobasidium pullulans α-amylase (ApAmy) mixed with melted agar-agar solution and drop-wisely added to a mixture of organic solvent solution allowed for the entrapment of the α-amylase in the agar-agar organic matrix as beads. The immobilized ApAmy’s characteristics and wash performance were elucidated in comparison with the soluble ApAmy. Agar-agar at 2.0 % (w/v) and toluene: chloroform at 3:1 resulted in the highest immobilization yield retaining about 98% residual activity after ten catalytic cycles. The optimum temperature and pH for the immobilized enzyme were 60ºC and 6.5 respectively. The immobilized ApAmy hydrolysed branched and linear substrates thus establishing its broad substrate specificity. Relatively, the immobilized ApAmy (iApAmy) was more tolerant to organic solvents than the free enzyme. The iApAmy was mildly inhibited by cobalt but metals such as zinc, manganese, calcium and sodium enhanced the free and immobilized ApAmy activity. The iApAmy had a higher washing efficiency (77%) in the presence of detergents than the free enzyme (68%) and control (36%). The iApAmy showed good potentials as a detergent additive and from its characteristics, it could be useful in other industrial applications. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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