Study on Purification of Lionleic Ismerase from Lactobacillus acidophilus

FOOD SCIENCE ›› 2007, Vol. 28 ›› Issue (12): 305-308.

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Study on Purification of Lionleic Ismerase from Lactobacillus acidophilus

WANG Wu, FU Min, TANG Xiao-Ming, PAN Jian

1.School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009, China; 2.Engineering Research Center of Bio-process, Ministry of Education, Hefei 230009, China

Online:2007-12-15 Published:2011-11-22

Abstract

Abstract: The purification of Lionleic ismerase in Lactobacillus acidophilus were studied in this paper. Crude enzyme from Lactobacillus acidophilus was purified by ammonium sulfate solution of 40%～80%, dialysis and Sephadex G-100 gel fractionation chromatography, achieving an overall purification of 3.10-fold and a spectic activity of 475.45[U/(mg protein)]. The purified enzyme was a single distinct protein band by SDS-PAGE, with an estimated molecular weight of about 46.6 kDa.

Key words: Lactobacillus acidophilus, lionleic ismerase, purification, SDS-PAGE

WANG Wu, FU Min, TANG Xiao-Ming, PAN Jian. Study on Purification of Lionleic Ismerase from Lactobacillus acidophilus[J]. FOOD SCIENCE, 2007, 28(12): 305-308.

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Study on Purification of Lionleic Ismerase from Lactobacillus acidophilus

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