So far, no salt-tolerant lipase has been described from lactic acid bacteria. In the
present study, the gene lp_3562 encoding a putative esterase/lipase was cloned and expressed in
Escherichia coli BL21 (DE3) and the overproduced Lp_3562 protein has been biochemically characterized.
Lp_3562 is a lipase active on tributyrin and also on other long chain substrates. Although the highest
activity was observed at pH 7, the enzyme showed activity at pH 5.0e8.0. Lp_3562 exhibited optimal
lipase activity at 40 C and, showing more than 40% of maximal activity at refrigeration temperature
(5 C). Conversely, Lp_3562 presented good thermostability exhibiting more than 80% of its maximal
activity after 20 h incubation at 45 C. More interestingly, Lp_3562 was active under NaCl concentrations
higher than 20%. The biochemical properties exhibited by Lp_3562 make this halotolerant lipase
attractive for its use in food fermentations.
So far, no salt-tolerant lipase has been described from lactic acid bacteria. In thepresent study, the gene lp_3562 encoding a putative esterase/lipase was cloned and expressed inEscherichia coli BL21 (DE3) and the overproduced Lp_3562 protein has been biochemically characterized.Lp_3562 is a lipase active on tributyrin and also on other long chain substrates. Although the highestactivity was observed at pH 7, the enzyme showed activity at pH 5.0e8.0. Lp_3562 exhibited optimallipase activity at 40 C and, showing more than 40% of maximal activity at refrigeration temperature(5 C). Conversely, Lp_3562 presented good thermostability exhibiting more than 80% of its maximalactivity after 20 h incubation at 45 C. More interestingly, Lp_3562 was active under NaCl concentrationshigher than 20%. The biochemical properties exhibited by Lp_3562 make this halotolerant lipaseattractive for its use in food fermentations.
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