Catalytic esterification performance of protease in micro-aqueous system.

Area of Science:

• Biocatalysis
• Enzyme Engineering
• Green Chemistry

Background:

• Proteases are versatile enzymes with potential applications in esterification reactions.
• Micro-aqueous systems offer unique environments for enzymatic catalysis.
• Optimizing enzyme activity in non-aqueous media is crucial for industrial applications.

Purpose of the Study:

• To assess the esterification performance of proteases in micro-aqueous systems.
• To determine optimal conditions for maintaining protease activity during esterification.
• To compare the esterification efficiency of proteases with lipases.

Main Methods:

• Enzymatic esterification reactions were conducted in micro-aqueous systems.
• The influence of boric acid-borax buffer concentration on protease activity was investigated.
• Enzyme activity was monitored under varying pH and temperature conditions.
• Sucrose-6-ethyl ester synthesis was performed using proteases and Candida lipase for comparative analysis.

Main Results:

• Protease exhibited superior catalytic activity in a micro-aqueous phase with 4% boric acid-borax buffer compared to a pure organic phase.
• Optimal protease activation was achieved with 0.20 M boric acid-borax buffer.
• Sustained high enzyme activity was observed at alkaline pH (8.40-9.60) and temperatures between 40-55 °C.
• Protease demonstrated higher esterification activity than Candida lipase in the micro-aqueous system for sucrose ester synthesis.

Conclusions:

• Proteases are effective biocatalysts for esterification in micro-aqueous systems.
• Boric acid-borax buffer significantly enhances protease activity and stability.
• The identified optimal conditions promote efficient and prolonged enzyme function.
• Proteases present a promising alternative to lipases for specific ester synthesis applications.