เอกสารการประชุมวิชาการและเสนอผลงานวิจัย มหาวิทยาลัยทักษิณ ครั้งที่ 19 2552 - page 894

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2552
protein were 44.38, 19.72 and 9.64 kDa. The salt phase was separated by Sephadex G 100 column and the
chromatogram showed 5 major protein peaks, second peak had lipase activity (0.121±0.007 Units/ml), while PEG
phase showed 8 major protein peaks, seventh peak had lipase activity (0.098±0.003 Units/ml). Two lipase activity
peaks were assumed to be 2 isozyme conformation in cocoanut had been purified by ATPS. The PEG phase lipase
was found to be stable in temperature range 50-80
o
C and at 80
o
C for 1 h the activity was 85.14 % but the salt
phase remain 67.04 %. The resultant from transesterification reaction by using PEG lipase(15.34 units/ml) as
biocatalytic synthesis of methyl esters at 40
o
C, maximum methyl esters yield was 75 % and this obtained
biodiesel had similarly physical and chemical property with biodiesel of NaOH catalyzing, to confirm obtained
biodiesel was used TLC, found that R
f
value of lipase biodiesel and base biodiesel to be approximately 0.71 and
0.78, the relative viscosity comparing with water was found 1.6 and 2.6 respectively.
Keywords :
Lipase; Aqueous two-phase systems, ATPS; Transesterification
;
biodiesel
;
relative viscosity
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