Full Length Research Paper
Abstract
An antarctic bacterial isolate displayed extracellular lipolytic activity. Based on the 16S rRNA sequence analysis, the strain was named Pseudomonas sp. INK1. The INK1 lipase was secreted into the production medium during transition to the stationary phase. The enzyme reached the apparent maximal activity at pH 8 to 9, with optimal activity at 50°C. The enzyme was active against a wide range of fatty acid esters of p-nitrophenyl, showing the highest activity towards p-nitrophenyl caprylate. It could also release caprylic acid from a natural substrate cream. The enzyme activity was strongly inhibited by Zn2+ and Mn2+, and slightly enhanced by EDTA. INK1 lipase may be a potentially useful catalyst to enhance the buttery flavor of dairy products.
Key words: Antarctic, lipolytic, Pseudomonas sp., catalyst, dairy products.
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