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ÝćÖ Hepatopancreas Öčš
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-JUPQFOBFVTǰWBOOBNFJ
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Biochemical Properties of Partially Purified Lipase
from Hepatopancreas of Pacific White Shrimp
-JUPQFOBFVTǰWBOOBNFJ
)
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Sakonwat Kuepethkaew
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, Kanokphorn Sangkharak
2
and Sappasith Klomklao
3*
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ÙǰThree phase-partitioning (TPP) øŠ
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ÙǰAqueous two-phase system (ATPS) óïüŠ
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Q
-nitrophenyl ester Āúć÷ßîĉ
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Q
-nitrophenyl acetate ÝćÖÖćøýċ
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üîÝćÖǰhepatopancreas Öčš
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Abstract
Lipase was partially purified from the hepatopancreas of Pacific white shrimp (
-JUPQFOBFVTǰ
WBOOBNFJ
) by three-phase partitioning (TPP) followed by simultaneous aqueous two-phase system
(ATPS). The biochemical properties of the partially purified lipase were also studied. The purified
enzyme exhibited optimal activity at pH 8.0 and 55
o
C and was stable at a temperature range of 0-40
o
C
and a pH range of 7.0-10.0. Activities of lipase continuously decreased as sodium deoxycholate (NaDC)
concentration increased. However, activities increased as NaCl concentration increased up to 3.0 M. It
hydrolyzed various
Q
-nitrophenyl ester with its highest activity on
Q
-nitrophenyl acetate. Base on
biochemical characterization studies, the partially purified lipase from hepatopancreas of Pacific white
shrimp can be used for certain food processing operations that require high alkaline and high salt
condition.
Keywords :
Lipase, Purification, Pacific White Shrimp, Viscera
1
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* Corresponding author: Tel.: 074-693996. E-mail address:
