Biochemical properties and positional specificity of Lipase from hepatopancreas of Tra catfish (Pangasius)
2013 ◽
Vol 16
(4)
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pp. 85-91
Keyword(s):
Lipase from the hepatopancreas of Tra catfish (Pangasius) was precipitated by ammonium sulfate fractionation, purified by ion-exchange chromatography on DEAE cellulose and gel filtration on Sephadex G- 75. On substrate triolein, purified lipase has Km= 1.381 mM and Vmax= 0.063 mM/min. The lipase was stable at a pH range of 7.0- 9.0 and in temperatures of 35-50°C. At 500C the enzyme loosed 44,7% activity after 120 min. The enzyme was specific for the α- positions (1, 3) of triglyceride. In bile salt solution of 0.015M NaTC, lipase activity of the enzyme increased in 3.08 folds in comparison of sample without NaTC.
1984 ◽
Vol 62
(6)
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pp. 449-455
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1982 ◽
Vol 49
(3)
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pp. 347-360
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2010 ◽
Vol 2010
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pp. 1-8
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1973 ◽
Vol 30
(02)
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pp. 414-424
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1990 ◽
Vol 36
(11)
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pp. 1906-1910
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2021 ◽
Vol 13
(2)
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pp. 107-112