A novel extracellular cold-active esterase of Pseudomonas sp. TB11 from glacier No.1: Differential induction, purification and characterisation

•Single cream was found as a good inducer for esterase to catalyze short and medium—a novel esterase from a psychrotolerant strain of glacier No.1 was purified and characterized.•Chain fat.•An improved zymography method was developed, which is simpler and faster.•It was proved EstTB11 had potential application in flavor development of dairy products.

The production, purification, characterization and application of a novel cold active esterase by Pseudomonas sp. TB11 are described herein. A new finding regarding the production of extracellular esterase activity depending upon single cream as an inducer used for growth was investigated in this study. The crude esterase was subjected to a three-step enzyme purification, which resulted in a 15.21-fold purification and the specific activity of the final purified esterase increased to 1526.2 U/mg protein and purified EstTB11 had a molecular mass of 65 kDa. The N-terminal sequence of ten amino acids were: GVYDYKNLTT. Peptide mass finger printing revealed that some peptides showed homologues sequences (29%) to polyurethanase of Pseudomonas sp. FH4. Furthermore, the enzyme displayed the optimum pH of 8.5 and optimum temperature of 25 °C and significantly high stability at 15–35 °C for 72 h. The enzyme was incubated with different metal ions at concentrations of 5 and 10 mM, the activity of esterase was increased in the presence of K+, Na+ and Mg2+ and decreased with Ca2+, Al3+, Mn2+, and Fe3+. Experiments indicated that EstTB11 could hydrolyze milk fat to produce short and medium-chain fatty acid and this result layed the foundation for the application in increased aroma of milk products.

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