Purification and partial characterization of polyphenol oxidase from the flower buds of Lonicera japonica Thunb.

被引:60
作者
Liu, Na-na [1 ,2 ]
Liu, Wei [1 ]
Wang, Dai-jie [1 ]
Zhou, Yi-bin [2 ]
Lin, Xiao-jing [1 ]
Wang, Xiao [1 ]
Li, Sheng-bo [3 ]
机构
[1] Shandong Acad Sci, Shandong Anal & Test Ctr, Jinan 250014, Shandong, Peoples R China
[2] Anhui Agr Univ, Coll Tea & Food Sci & Technol, Hefei 230036, Anhui, Peoples R China
[3] Shandong Yate Ecol Technol Co Ltd, Linyi 276017, Shandong, Peoples R China
关键词
Lonicera japonica; Polyphenol oxidase; Purification; Characterization; L;
D O I
10.1016/j.foodchem.2012.10.103
中图分类号
O69 [应用化学];
学科分类号
070301 [无机化学];
摘要
The purification and partial enzymology characteristics of polyphenol oxidase from Lonicera japonica (LjPPO) were studied in this paper. The crude enzyme solution was purified in turn by ammonium sulfate, dialysis, and DEAE-cellulose ion-exchange chromatography after preliminary treatments. Purification resulted in 31-fold enrichment and its molecular weight was estimated to be similar to 49 kDa exhibited on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The pH for optimal conditions of LjPPO was 7.5, and the temperature was 25 degrees C, in addition, the inhibitive effects of inhibitors were enhanced positively with increasing of the concentration. Moreover, crude enzyme solution showed diphenolase activity toward catechol, L-dopa and chlorogenic acid rather than monophenolase and tri-phenolase activity, and the best substrate was catechol because of the highest V-max/K-m value. However, the oxidation of diphenol related to browning significantly, so the data obtained in this research provided theoretical basis for the prevention of enzymatic browning of L. japonica during processing. (C) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码:478 / 483
页数:6
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