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 storage
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.
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 storage
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.
| Original language | English |
|---|---|
| Article number | E6 |
| Number of pages | 10 |
| Journal | Trends in Protein and Peptide Science |
| Volume | 4 |
| DOIs | |
| Publication status | Published - 1 Jan 2019 |
Keywords
- Calcium alginate
- Enzyme entrapment
- Enzyme reusability
- Enzyme stability
- Lipase