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Abstract

Lipolytic activity was assayed in samples of Antarctic krill frozen in different conditions and in its liquid digesta with synthetic (tributylglycerol, esters of 2-naphtol and fatty acids C3, C9 , C14 and C18 ) and natural (olive oil) substrates. It was testified that the lipolytic activity is several-fold higher in the crustaceans with high food intake than in those with an empty digestive tract. Krill lipases show higher activity against esters of unsaturated fatty acids that against analogous derivatives of saturated ones and 10-fold higher affinity tributylglycerol (Km = 1.12 mM). Their maximal activity is at pH 6.4 and 37°C. E. superba lipases preserve total activity up to 35°C for 45 minutes, and are completely inactivated at 55°C for 5 minutes. Prevailing part of lipolytic activity is present in krill cephalothorax, however, extracts from krill abdomen also display a marked activity. Krill lipases are probably resistant to an attack of crustacean's proteinases.
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Abstract

The marine psychrophilic and endemic Antarctic yeast Leucosporidium antarcticum strain 171 synthesizes intracellular b-fructofuranosidase, and intra- and extracellular a-glucosidases. Each enzyme is maximally produced at 5°C , while the strain’s optimum growth temperature is 15°C . Invertase biosynthesis appeared regulated by catabolic repression, and induced by sucrose; the enzyme was extremely unstable ex vivo, and only EDTA, Mn2+, and BSA stabilized it for up to 12 h after yeast cell lysis. Thermal stability of the invertase was also low (30 min at temperatures up to 12°C). The optimum temperature for invertase activity was 30°C , and optimum pH was 4.55 to 4.75. The extracellular a-glucosidase was maximally active at 35°C and pH 6.70–7.50, and stable for 30 min up to 20°C.
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