2015
DOI: 10.1002/bab.1445
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A newly thermoactive and detergent‐stable lipase from annular sea bream (Diplodus annularis): Biochemical properties

Abstract: A lipolytic activity was located in the annular seabream pyloric caeca, from which a digestive lipase (AsDL) was purified. Pure AsDL has an apparent molecular mass of 50 kDa. The purified lipase is thermoactive as it displays its maximal activity on short- and long-chain triacylglycerols at a temperature of 50 °C. The enzyme is alkaline resistant as it retains 90% of its maximal activity when incubated during 1 H at pH 10. No colipase was detected in the annular seabream pyloric caeca. Similar results were rep… Show more

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Cited by 6 publications
(11 citation statements)
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“…Interestingly, the fish enzyme preserved 95% of its maximal activity in the presence of high concentrations of NaDC. Similar results were previously obtained with purified lipase from the annular seabream and other digestive lipases isolated from sardine and crab . Furthermore, this behavior is different from that of stingray pancreatic lipase, which showed an absolute requirement for bile salts .…”
Section: Resultssupporting
confidence: 87%
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“…Interestingly, the fish enzyme preserved 95% of its maximal activity in the presence of high concentrations of NaDC. Similar results were previously obtained with purified lipase from the annular seabream and other digestive lipases isolated from sardine and crab . Furthermore, this behavior is different from that of stingray pancreatic lipase, which showed an absolute requirement for bile salts .…”
Section: Resultssupporting
confidence: 87%
“…The enzyme apparent molecular mass is about 50 kDa. This is in line with the molecular mass of AsDL .…”
Section: Resultssupporting
confidence: 84%
See 3 more Smart Citations