Partial Purification and Characterization of Latent Polyphenol Oxidase in Iceberg Lettuce (LactucasativaL.)

1996 ◽  
Vol 44 (4) ◽  
pp. 984-988 ◽  
Author(s):  
Soledad Chazarra ◽  
Juana Cabanes ◽  
Josefa Escribano ◽  
Francisco Garcia-Carmona
Keyword(s):  
Polyphenol Oxidase ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Iceberg Lettuce

Partial Purification and Characterization of Polyphenol Oxidase Isozymes in Banana Bud

1992 ◽  
Vol 56 (7) ◽  
pp. 1027-1030 ◽  
Author(s):  
Kazuko Ôba ◽  
Norio Iwatsuki ◽  
Ikuzo Uritani ◽  
Angelina M. Alvarez ◽  
Virgilio V. Garcia
Keyword(s):  
Polyphenol Oxidase ◽  
Partial Purification ◽  
Purification And Characterization

Partial Purification and Characterization of Polyphenol Oxidase from Banana (Musa sapientumL.) Peel

2001 ◽  
Vol 49 (3) ◽  
pp. 1446-1449 ◽  
Author(s):  
Chang-Peng Yang ◽  
Shuji Fujita ◽  
Koei Kohno ◽  
Akiko Kusubayashi ◽  
MD. Ashrafuzzaman ◽  
...  
Keyword(s):  
Polyphenol Oxidase ◽  
Partial Purification ◽  
Purification And Characterization

Partial Purification and Characterization of Polyphenol Oxidase Extracted from Agaricus bisporus (J.E.Lange) Imbach

2007 ◽  
Vol 5 (1) ◽  
Author(s):  
Hicham Gouzi ◽  
Abdelhafid Benmansour
Keyword(s):  
Polyphenol Oxidase ◽  
Agaricus Bisporus ◽  
Mixed Type ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Heat Stable ◽  
Monophenolase Activity ◽  
Specificity Constant ◽  
Diphenolase Activity

Polyphenol oxidase (PPO) from mushrooms (Agaricus bisporus (J.E.Lange) Imbach) was partially purified and characterized. The enzyme exhibited both monophenolase and diphenolase activities that were measured spectrophotometrically using L-tyrosine and pyrogallol as substrates. A two-fold purification in both activities was achieved by ammonium sulfate fractionation. The monophenolase activity was 3.35 EU/ml, and the diphenolase activity was 189.3 EU/ml. PPO was relatively stable at -15°C for 44 days. The enzyme was not very heat stable, and its activity decreased when incubated at the temperatures higher than 35°C. PPO activity showed two pH optima, at 5.3 and 7.0 at 25°C when pyrogallol was used as the substrate.Mono-, di- and triphenols were substrates for PPO. Using Vmax/Km as a specificity constant, pyrocatechol was the better substrate followed by pyrogallol. The kinetic parameters of the enzyme were: Vmax = 78 EU/min/ml, Km = 1.4 mM and KS = 250 mM for pyrogallol and Vmax = 168 EU/min/ml, Km = 0.40 mM and KS = 270 mM for the pyrocatechol. Of the inhibitors tested, competitive-type inhibition was observed with benzoic acid and sodium azide. A mixed-type inhibition was observed with L-cysteine and sodium fluoride.

Partial purification and characterization of polyphenol oxidase from persimmon

2014 ◽  
Vol 157 ◽  
pp. 283-289 ◽  
Author(s):  
José L. Navarro ◽  
Amparo Tárrega ◽  
Miguel A. Sentandreu ◽  
Enrique Sentandreu
Keyword(s):  
Polyphenol Oxidase ◽  
Partial Purification ◽  
Purification And Characterization

Partial purification and characterization of polyphenol oxidase and peroxidase from chestnut kernel

LWT ◽  
2015 ◽  
Vol 60 (2) ◽  
pp. 1095-1099 ◽  
Author(s):  
Zhiqing Gong ◽  
Dajing Li ◽  
Chunquan Liu ◽  
Anwei Cheng ◽  
Wenliang Wang
Keyword(s):  
Polyphenol Oxidase ◽  
Partial Purification ◽  
Purification And Characterization
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