Lipolysis of different oils using crude enzyme isolate from the intestinal tract of rainbow trout, Oncorhynchus mykiss
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Lipolysis of different oils using crude enzyme isolate from the intestinal tract of rainbow trout, Oncorhynchus mykiss. / Gøttsche, Jesper; Nielsen, Nina Skall; Nielsen, Henrik; Mu, Huiling.
I: Lipids, Bind 40, Nr. 12, 2005, s. 1273-9.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Lipolysis of different oils using crude enzyme isolate from the intestinal tract of rainbow trout, Oncorhynchus mykiss
AU - Gøttsche, Jesper
AU - Nielsen, Nina Skall
AU - Nielsen, Henrik
AU - Mu, Huiling
PY - 2005
Y1 - 2005
N2 - Crude enzyme isolate was prepared from the intestine of rainbow trout. Positional specificity of the crude enzyme isolate was determined from both 1(3)- and 2-MAG products after in vitro lipolysis of radioactive-labeled triolein. The ratio of 2-MAG/1(3)-MAG was 2:1, suggesting that the overall lipase specificity of the enzyme isolate from rainbow trout tended to be 1,3-specific; however, activity against the sn-2 position also was shown. In vitro lipolysis of four different unlabeled oils was performed with the crude enzyme isolate. The oils were: structured lipid [SL; containing the medium-chain FA (MCFA) 8:0 in the sn-1,3 positions and long-chain FA (LCFA) in the sn-2 position], DAG oil (mainly 1,3-DAG), fish oil (FO), and triolein (TO). MCFA were rapidly hydrolyzed from the SL oil. LCFA including n-3 PUFA were, however, preserved in the sn-2 position and therefore found in higher amounts in 2-MAG of SL compared with 2-MAG of FO, DAG, and TO. Lipolysis of the DAG oil produced higher amounts of MAG than the TAG oils, and 1(3)-MAG mainly was observed after lipolysis of the DAG oil. The positional specificity determined and the results from the hydrolysis of the different oils suggest that n-3 very long-chain PUFA from structured oils may be used better by aquacultured fish than that from fish oils.
AB - Crude enzyme isolate was prepared from the intestine of rainbow trout. Positional specificity of the crude enzyme isolate was determined from both 1(3)- and 2-MAG products after in vitro lipolysis of radioactive-labeled triolein. The ratio of 2-MAG/1(3)-MAG was 2:1, suggesting that the overall lipase specificity of the enzyme isolate from rainbow trout tended to be 1,3-specific; however, activity against the sn-2 position also was shown. In vitro lipolysis of four different unlabeled oils was performed with the crude enzyme isolate. The oils were: structured lipid [SL; containing the medium-chain FA (MCFA) 8:0 in the sn-1,3 positions and long-chain FA (LCFA) in the sn-2 position], DAG oil (mainly 1,3-DAG), fish oil (FO), and triolein (TO). MCFA were rapidly hydrolyzed from the SL oil. LCFA including n-3 PUFA were, however, preserved in the sn-2 position and therefore found in higher amounts in 2-MAG of SL compared with 2-MAG of FO, DAG, and TO. Lipolysis of the DAG oil produced higher amounts of MAG than the TAG oils, and 1(3)-MAG mainly was observed after lipolysis of the DAG oil. The positional specificity determined and the results from the hydrolysis of the different oils suggest that n-3 very long-chain PUFA from structured oils may be used better by aquacultured fish than that from fish oils.
M3 - Journal article
C2 - 16477812
VL - 40
SP - 1273
EP - 1279
JO - Lipids
JF - Lipids
SN - 0024-4201
IS - 12
ER -
ID: 44090650