Isolation, Purification and Characterization of Acid Phosphatase from Cilantro

doi:10.7506/spkx1002-6630-201521031

Abstract

Abstract:

Electrophoresis-purity acid phosphatase (ACP) from cilantro was obtained by homogenization, buffer solutionextraction, ammonium sulfate fractional precipitation, CM-Sepharose ion exchange chromatography and Superdex-200 gelfiltration. The results showed that after purification the recovery rate of ACP activity was 14.20% with a purification fold of238.60, and the specific activity of ACP was 295.87 U/mg. The subunit molecular mass of the enzyme was approximately53.8 kD. The characterization of ACP illustrated that the optimal reaction temperature was 55 ℃, and it was stable inthe range of 20–50 ℃. Therefore, the enzyme was sensitive to temperature. The optimal reaction pH was 5.8, and it wasrelatively stable in the range of pH 4.0–7.0. The enzyme showed tolerance to acidic environment. Its Km was 0.63 mmol/Ltowards p-nitrophenyl phosphate disodium salt hexahydrate, indicating high affinity between the enzyme and the substrate.The enzyme activity of ACP could be strongly inhibited by methanol, ethanol, isopropanol, ascorbic acid, oxalic acid andCu2+, Pb2+ and Ag+, while it could be enhanced to some extent by Mg2+, Mn2+, Ba2+ and K+.

Key words: cilantro, acid phosphatase, isolation and purification, enzymatic properties

CLC Number:

Q946.5

WANG Dan, WAN Ji, FU Ting, TANG Yunming. Isolation, Purification and Characterization of Acid Phosphatase from Cilantro[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201521031.

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Isolation, Purification and Characterization of Acid Phosphatase from Cilantro

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