Catalyzed Ester Synthesis UsingCandida rugosaLipase Entrapped by Poly(N-isopropylacrylamide-co-itaconic Acid) Hydrogel

Abstract

This study reports the synthesis of polymeric matrices based on N-isopropylacrylamide and itaconic acid and its application for immobilization of lipase from Candida rugosa. The lipase was immobilized by entrapment method. Free and immobilized lipase activities, pH and temperature optima, and storage stability were investigated. The optimum temperature for free and entrapped lipase was found to be 40 and 45°C, while the optimum pH was observed at pH 7 and 8, respectively. Both hydrolytic activity in an aqueous medium and esterolytic activity in an organic medium have been evaluated. Maximum reaction rate (V max) and Michaelis-Menten constants (K m) were also determined for immobilized lipase. Storage stability of lipase was increased as a result of immobilization process. Furthermore, the operational stability and reusability of the immobilized lipase in esterification reaction have been studied, and it was observed that after 10 cycles, the residual activity for entrapped lipase was as high as 50%, implying that the developed hydrogel and immobilized system could provide a promising solution for the flavor ester synthesis at the industrial scale.

Biomass-Derived Production of Itaconic Acid as a Building Block in Specialty Polymers

“…In water or wastewater treatment, there is growing interest in the utilization of hydrogels that offer positive results in the removal of aqueous pollutants. The copolymerization of IA with different natural biopolymers usually improves the hydrogel structure and increases the degree of crosslinking [141,144]. Nevertheless, the essential challenges are in resource recovery, regeneration, reusability, and recovery of hydrogels [145].…”

Substrate-Specificity ofCandida rugosaLipase and Its Industrial Application

“…Entrapment immobilization is, as adsorption, a physical immobilization method, in which there are no covalent interactions between the lipase and the support. CRL will be captured within a polymeric network that allows the substrates and products to pass through but retains the enzyme. , Various matrices can be used for entrapment of lipases, such as chitosan, calcium alginate, collagen, cellulose triacetate, poly acrylamide, gelatin, agar, silicon rubber, poly­(vinyl alcohol) and polyurethane. − There are different approaches to entrap enzymes such as gel/fiber inclusion or microencapsulation. − The latter method, microencapsulation, is more complicated as the technique mentioned above and immobilizes a large quantity of enzymes by enclosing them within spherical semipermeable polymer membranes with controlled porosity (1–100 μm) . There are a lot of advantages with entrapment.…”

Recent advances on sources and industrial applications of lipases

“…Apart from using organic solvents for the reaction, lipase‐catalyzed hydrolytic reactions can also be performed in aqueous environment contributing to greener processes . These esterolytic reactions have a great potential in the synthesis of wide range of products such as of polymeric matrices based on N ‐isopropylacrylamide and itaconic acid using immobilized lipase from C. rugosa . Further, lipase from C. rugosa was used to catalyze racemic esterolytic reaction of high oleate sunflower oil to produce glycerol and corresponding free fatty acid .…”

“…191 These esterolytic reactions have a great potential in the synthesis of wide range of products such as of polymeric matrices based on N-isopropylacrylamide and itaconic acid using immobilized lipase from C. rugosa. 192 Further, lipase from C. rugosa was used to catalyze racemic esterolytic reaction of high oleate sunflower oil to produce glycerol and corresponding free fatty acid. 193 Also, infant milk formulae are produced using lipase as hydrolytic catalyst.…”