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Biochemical characterization with kinetic studies of melanogenic enzyme tyrosinase from white button mushroom, Agaricus bisporus

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Title Biochemical characterization with kinetic studies of melanogenic enzyme tyrosinase from white button mushroom, Agaricus bisporus
 
Creator Kaur, Ravneet
Sharma, Shivani
Kaur, Satvir
Sodhi, HS
 
Subject Enzyme Inhibitors
FTIR
Ion exchange chromatography
SDS-PAGE
Substrate specificity
 
Description 718-725
In Agaricus bisporus, color is a key determinant for marketability and consumer acceptability. However, postharvest
browning has become a major concern, affecting the overall economics of the mushroom industry. In button mushrooms, the
tyrosinase enzyme (E.C.1.14.18.1) is responsible for the browning reactions by catalyzing the conversion of monophenols
and diphenols into quinones which polymerize to form melanin. Thus, the present study focused on the purification and
characterization of tyrosinase from A. bisporus. This enzyme was purified with a final yield of 19.71% and 32.05
purification fold. The study of enzymatic activity over a temperature (5-45°C) and pH range (3-10) showed that the
optimum temperature was 35°C with pH 7. The kinetic studies revealed that Km values were different for catechol
(0.71 mM) and L-dopa (0.87 mM), which indicated a higher affinity of the enzyme for catechol. Inhibition studies showed
that cinnamic acid is a non-competitive inhibitor while salicylic acid is a competitive inhibitor of tyrosinase. The molecular
weight of the enzyme was found to be 43 kDa and different amide regions were reflected by the FTIR spectra of the
enzyme. This study may provide valuable insights into the structure, biochemical properties, and inhibition of tyrosinase
enzyme for controlling mushroom browning.
 
Date 2022-08-01T06:58:05Z
2022-08-01T06:58:05Z
2022-07
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://nopr.niscpr.res.in/handle/123456789/60229
 
Language en
 
Publisher NIScPR-CSIR,India
 
Source IJBB Vol.59(7) [July 2022]