Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

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.

Preparation and characterization of sugilite glass from basalt for α-amylase immobilization, statistical optimization of the immobilization process and description of free and immobilized enzyme

“…In general, a carrier is considered ideal when it is low cost, high physical and chemical stability, good biocompatibility, and having many points for enzyme attachment (Remonatto et al, 2021). Inorganic carriers are proper for industrial applications because they are inert, affordable, non-toxic, insoluble, have physical strength, regeneration, stability, ability to increase enzyme activity/specificity and diminish product inhibition (Datta et al, 2013;Ahmed et al, 2018;Ricardia et al, 2018).…”

Solvent-Free Enzymatic Synthesis of Dietary Triacylglycerols from Cottonseed Oil in a Fluidized Bed Reactor

“…The integrals of Equations ( 6) and (7) were resolved using Origin software version 8.0 (OriginLab serial GA3S5-6089-7173339, Northampton, MA, USA). For analysis of preferential flow pathways, the results of space time (theoretical, Equation ( 8)) were compared with the mean residence time (experimental, Equation ( 7)).…”

“…These enzymes typically catalyze the hydrolysis of triacylglycerols into fatty acids and glycerol. Under non-aqueous conditions, however, lipases are capable of catalyzing esterification, transesterification, aminolysis, interesterification, and acidolysis reactions on a wide variety of substrates [ 3 , 4 , 5 , 6 , 7 ]. Another interesting characteristic of lipases is their ability to act on the different ester bonds of triacylglycerol, which makes it possible to control the incorporation and distribution of fatty acids in the glycerol backbone, a fundamental mechanism for the production of structured lipids.…”

Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications

“…Despite many common features, different nanomaterials exhibit different effects on enzymatic structures or activities, depending Detailed information on the features, properties and application of the different materials used for multienzymes immobilization can be found in recently published reviews [148,173,197,198]. Carbon-based materials, ceramics (e.g., kaolinite, montmorillonite) [199], metal oxides (e.g., alumina [200], titanium oxide [201], zirconia [202]), magnetic particles (maghemite, magnetite) [203], inorganic sol-gel, e.g., silica-based sol-gel, [204] silica, silica derivatives and siliceous materials [205], porous glass [206], pumice stone [207] Organic materials:…”