Background: Cross-linked enzyme aggregate (CLEA) is considered as an effective technique in the production of immobilized biocatalysts for its industrially attractive advantages. Simplicity, stability, low cost, time saving and reusability are proved to be some of CLEA's main advantages.
Results:In this study, an active, stable and recyclable CLEA-protease from the viscera of channel catfish Ictalurus punctatus has been prepared. Optimization of the preparation parameters is carried out with the help of Response Surface Methodology. This methodology helped in studying the interaction between the most contributing factors such as cross-linker, precipitant and the additive concentrations. The optimum specific activity for CLEA-protease of 4.512 U/mg protein has shown a high stability against the denaturation forces such as temperature and pH as compared to free protease. It is further found from the study that the highest activity was achieved at the pH of 6.8 and at the temperature of 45 °C. After six cycles, CLEA-protease maintained 28 % of its original activity. Additionally, Michaelis-Menten models were used to determine the kinetic parameters i.e. K m and V max that helped in showing a significant difference after immobilization as compared to free protease.
Conclusion:This work found that this novel CLEA-protease can be used as a very active biocatalyst in industrial applications.
Cocoa pod husk (CPH) is a by-product of cocoa production obtained
after removing the beans from the fruit. The analysis of CPH has shown that it
contains high amounts of protein. This study is aimed to utilize this protein source
in hydrolase enzyme production. In this study, seven hydrolase enzymes (amylase,
fructosyltransferase, mannanase, glucosidase, glucanase, lipase and protease) were
screened from CPH for the first time for feasible industrial production. Among these
hydrolases, lipase was chosen for the next steps of experiments as it has a lot of
applications in different industries. The extraction of high active lipase from CPH
has been done under optimum conditions. The condition that was optimum for the three
major factors was achieved using Face centered central composite design (FCCCD) with
response surface methodology (RSM) to obtain the highest enzyme activity of crude
lipase from CPH. The optimum condition of extraction is used for preparation of
cross-linked enzyme aggregate (CLEA). For the production of immobilized biocatalyst,
the technique of CLEA is considered as an effective technique for its industrially
attractive advantages. Referring to the results of OFAT, CLEA-lipase was prepared in
the best condition at the presence of 30 mM ammonium sulphate, 70 mM glutaraldehyde
with 0.23 mM Bovine serum albumin as an additive. Immobilization effectively
improved the stability of lipase against various organic solvents.
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