The Effect of Calcium Alginate Entrapment on the Stability of Novel Lipases from P. Reinekei and P. brenneri

Abstract

The high cost of soluble enzymes can limit their use for commercial and industrial purposes. Immobilization can enhance enzyme reusability, thereby reducing product isolation costs and overcoming this economic barrier. In the current study, two novel, purified lipases from Pseudomonas sp. (Pseudomonas reinekei and Pseudomonas brenneri) were entrapped in a calcium alginate matrix, with the aim of simultaneously enhancing enzyme reusability and stability. Following entrapment, the retained activity of the enzyme-alginate composite was verified by an enzymatic hydrolysis reaction of a p-nitrophenol palmitate substrate. The effect of the enzyme-alginate entrapment against various physiochemical parameters such as pH, temperature, metal ions, and solvents were subsequently examined. The entrapment was found to have minimal beneficial stability gains. However, enhanced enzyme reusability (up to 3 cycles) and stability (up to 18 days at 4°C) of the calcium alginate entrapped lipase, as indicated by residual hydrolysis of p-nitrophenol palmitate, was observed, suggesting potential roles for calcium alginate entrapped lipases in cost efficient enzyme catalysis. HIGHLIGHTS •Two novel lipases have been entrapped in calcium alginate for the first time. •A statistically enhanced stability in 1M EDTA was observed following entrapment. •The novel entrapped lipases display excellent storage stability and reusability.

Keywords

• calcium alginate
• enzyme entrapment
• enzyme reusability
• enzyme stability
• lipase