Immobilization of Pancreatic Lipase on Polyvinyl Alcohol by Cyanuric Chloride

Abstract

Porcine pancreatic lipase (EC 3.1.1.3) was covalently immobilized onto 2,4,6-trichloro-s-triazine (cyanuric chloride) activated polyvinyl alcohol (PVA). The influence of activating agent and enzyme concentration on the immobilization process were evaluated. Hydrolytic activities of free and immobilized enzyme were determined and the immobilization yield was estimated by measuring the quantity of protein, both in free enzyme solution and in washing solutions after immobilization. After the optimization of immobilization process, the physical and chemical characterization of immobilized enzyme was performed. Additionally, the thermal, pH, storage, and operational stability of the immobilized and free enzymes were tested. Obtained data showed that the immobilized enzyme seemed better and offered some advantages in comparison with free enzyme.

Crosslinked aggregates of Rhizopus oryzae lipase as industrial biocatalysts: Preparation, optimization, characterization, and application for enantioselective resolution reactions

“…A pH gradient between the immobilized lipase particles' domains and the external solution is formed during the enzymatic hydrolysis reaction shifting the optimum pH toward the alkaline region. Similar pH shifts to the alkaline region through positively charged groups for immobilized enzymes have been reported previously by many researchers 44, 46–49…”

Immobilization of Lipase on Silver Nanoparticles via Adhesive Polydopamine for Biodiesel Production

“…Significantly, at high temperatures of 45, 50, and 55°C, immobilized lipase activities were higher than those of soluble lipase from approximately 10 to 20%. It was identical to 2,4,6-trichloro-s-triazine activated polyvinyl alcohol-immobilizing porcine pancreatic lipase [46]. By means of this, our work contributes to knowledge of lipase immobilization with regards to temperature resistance since over 80% relevant works use immobilized lipases [8].…”

Efficient Display of Aspergillus niger β-Glucosidase on Saccharomyces cerevisiae Cell Wall for Aroma Enhancement in Wine

“…13 However, we observed this phenomenon only when glucose concentrations were below 5.0% (Figure 3A). Enzymes immobilized on solid supports by chemical binding, physical retention, or biomolecular affinity binding exhibit shifts in pH, stability ranges, and increased resistance to inactivation by pH, 32,33 similar to the enhanced stability of BGL on yeast cell surface via an anchor protein at low pH. Based on these previous reports, proteins attached to the cell surface appear to be more stable than proteins in solution and are more resistant to external factors.…”