Abstract
Lipase is an important group of biocatalysts, which combines versatility and specificity, and can catalyze several reactions when applied in a high amount of industrial processes. In this study, the lipase produced by Aspergillus japonicus under submerged cultivation, was immobilized by physical adsorption, using clay supports, namely, diatomite, vermiculite, montmorillonite KSF (MKSF) and kaolinite. Besides, the immobilized and free enzyme was characterized, regarding pH, temperature and kinetic parameters. The most promising clay support was MKSF that presented 69.47% immobilization yield and hydrolytic activity higher than the other conditions studied (270.7 U g−1). The derivative produced with MKSF showed high stability at pH and temperature, keeping 100% of its activity throughout 12 h of incubation in the pH ranges between 4.0 and 9.0 and at a temperature from 30 to 50 °C. In addition, the immobilized lipase on MKSF support showed an improvement in the catalytic performance. The study shows the potential of using clays as support to immobilized lipolytic enzymes by adsorption method, which is a simple and cost-effective process.
Highlights
Lipases [EC 3.1.1.3] are enzymes that hydrolyze ester linkages of triglycerides [1,2]
These results are in accordance with those (20.6 U ml−1) obtained by Karanam et al [44] in the hydrolysis of p-nitrophenyl palmitate by a lipase preparation using a genetically modified strain of A. japonicus MTCC 1975
There is a wide range of process that immobilized enzymes can be applied and the results reported in the present work demonstrate that the low cost montmorillonite KSF (MKSF) is a promising support for A. japonicus lipase, and can encourage the scientific community to explore other clays-based substrates for enzymes immobilization, providing a natural and economical support to the industrial application of immobilized enzyme
Summary
Lipases ( triacylglycerol ester hydrolase) [EC 3.1.1.3] are enzymes that hydrolyze ester linkages of triglycerides [1,2] Since these enzymes present large structural and functional versatility, they are of greatest importance in industrial sector to be applied in the food, pharmaceutical, detergent, textile, biodiesel production, cosmetic, among others [3,4]. The industrial needs for new microbial sources of lipases with different catalytic characteristics [11] encouraged the search of new strains, viz, A. japonicus. In this sense, following the selection of lipase-strain producer, the enzyme immobilization its necessary, as it allows easy control of reaction parameters (flow rate and substrates), reuse of immobilized catalysts and suitable chemical, mechanical and thermal stability [3,12]
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