Purification and Enzymatic Properties of Cryogenic Lipase
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    Abstract:

    A lipase from Bacillus thuringiensis CZW001 was purified to homogeneity using ammonium sulfate precipitation,dialysis,DEAE-cellulose-52 anion exchange chromatography and Sephadex G-75 gel filtration chromatography.This purification protocol resulted in a 75.5 fold purification of lipase with 37.6% final yield,and the relative molecular weight of the enzyme was determined to be approximately 40kD using SDS-PAGE.Preliminary stuies have shown that the enzymatic properties of bacteria lipase,the enzyme’s optimum temperature is 25 ℃ and the enzyme was thermal lability,only 30% of its activity was remained after 30 min incubation at 60 ℃.The enzyme showed high lipolytic from ph 7.0 to 9.0 and its optimal ph for activity was 8.0.Ca2+ions stimulated lipolytic activity,whereas Al3+、Zn2+and Fe2+ions caused inhibition.Lipase tolerance of organic solvents of alcohols with carbon chain decreases.Lipase on soybean oil showed a significant the hydrolysis of the lipase.

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WANG Chun-yu, CHI Nai-yu, ZHANG Qing-fang, DOU Shao-hua. Purification and Enzymatic Properties of Cryogenic Lipase[J]. Journal of Food Science and Biotechnology,2013,32(8):809-813.

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History
  • Received:October 30,2012
  • Revised:
  • Adopted:
  • Online: October 28,2013
  • Published: August 25,2013
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