Characterization of polyphenol oxidase from blueberry (Vaccinium corymbosum L.).

Abstract:

:Polyphenol oxidase (PPO) was extracted and characterized from high-bush blueberries. PPO showed an optimum activity at pH 6.1-6.3 and 35°C, with the enzyme showing significant activity over a wide temperature range (25-60°C). Catechol was the most readily oxidized substrate followed by 4-methylcatechol, DL-DOPA, and dopamine. Blueberry PPO showed a Km of 15mM and Vmax of 2.57 ΔA420nm/min×10-1, determined with catechol. PPO was completely inactivated in 20min at 85°C, however, after 30minat 75°C it showed about 10% residual activity. Thermal treatment at 55 and 65°C for 30min resulted in the partial inactivation of PPO. Ascorbic acid, sodium diethyldithiocarbamic acid, L-cysteine, and sodium metabisulfite were effective inhibitors of PPO at 1.0mM. Benzoic acid and cinnamic acid series inhibitors showed relatively weak inhibition of PPO (21.8-27.6%), even at as high as 2.0mM concentration.

journal_name

Food Chem

journal_title

Food chemistry

authors

Siddiq M,Dolan KD

doi

10.1016/j.foodchem.2016.09.061

subject

Has Abstract

pub_date

2017-03-01 00:00:00

pages

216-220

eissn

0308-8146

issn

1873-7072

pii

S0308-8146(16)31443-1

journal_volume

218

pub_type

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