Changes in activity, structure and morphology of horseradish peroxidase induced by cold plasma.

08:00 EDT 23rd July 2019 | BioPortfolio

Summary of "Changes in activity, structure and morphology of horseradish peroxidase induced by cold plasma."

Cold plasma is an emerging technology increasingly applied in the agri-food industry. For fruit and vegetables, enzymatic browning is a common phenomenon, causing quality deterioration. The objective of this study was to illustrate the effect of microscale atmospheric-pressure plasma jet (µAPPJ) plasma on the horseradish peroxidase (HRP). Results showed that after plasma treatment for 10 min, the residual activity of HRP was decreased to around 17%, and modification of secondary and tertiary structures were confirmed. The atomic force microscope (AFM) analysis revealed that the aggregation of enzyme protein was enhanced with prolonging treatment time. It was concluded that the activity of HRP could be reduced with destruction of structures and deformation of microstructure induced by µAPPJ plasma. The current study attempted to provide new idea for inhibiting browning enzymes of fruit and vegetables with plasma technology through deeper understanding of the interaction mechanism of plasma active species with enzymes.


Journal Details

This article was published in the following journal.

Name: Food chemistry
ISSN: 1873-7072
Pages: 125240


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Medical and Biotech [MESH] Definitions

The lectin wheatgerm agglutinin conjugated to the enzyme HORSERADISH PEROXIDASE. It is widely used for tracing neural pathways.

An enzyme isolated from horseradish which is able to act as an antigen. It is frequently used as a histochemical tracer for light and electron microscopy. Its antigenicity has permitted its use as a combined antigen and marker in experimental immunology.

A 66-kDa peroxidase found in EOSINOPHIL granules. Eosinophil peroxidase is a cationic protein with a pI of 10.8 and is comprised of a heavy chain subunit and a light chain subunit. It possesses cytotoxic activity towards BACTERIA and other organisms, which is attributed to its peroxidase activity.

An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.

A plant genus of the family BRASSICACEAE known for the root used in hot SPICES and is the source of HORSERADISH PEROXIDASE which is widely used in laboratories.

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