Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates

Numerous reports illustrate the diverse effects of chewing the areca nut, most of which are harmful and have been shown to be associated with oral cancer. Nearly all of the studies are focused on the extract and/or low molecular weight ingredients in the areca nut. The purpose of this report is to i...

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Main Authors:	Liu, Yu-Ching, Chen, Chao-Jung, Lee, Miau-Rong, Li, Mi, Hsieh, Wen-Tsong, Chung, Jing-Gung, Ho, Heng-Chien
Format:	Online
Language:	English
Published:	Hindawi Publishing Corporation 2013
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3821912/

id	pubmed-3821912
recordtype	oai_dc
spelling	pubmed-38219122013-11-18 Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates Liu, Yu-Ching Chen, Chao-Jung Lee, Miau-Rong Li, Mi Hsieh, Wen-Tsong Chung, Jing-Gung Ho, Heng-Chien Research Article Numerous reports illustrate the diverse effects of chewing the areca nut, most of which are harmful and have been shown to be associated with oral cancer. Nearly all of the studies are focused on the extract and/or low molecular weight ingredients in the areca nut. The purpose of this report is to identify the major protein component in the areca nut. After ammonium sulfate fractionation, the concentrated areca nut extract is subjected to DEAE-cellulose chromatography. A colored protein is eluted at low NaCl concentration and the apparently homogeneous eluent represents the major protein component compared to the areca nut extract. The colored protein shares partial sequence identity with the royal palm tree peroxidase and its peroxidase activity is confirmed using an established assay. In the study, the natural substrates of areca nut peroxidase are identified as catechin, epicatechin, and procyanidin B1. The two former substrates are similarly oxidized to form a 576 Da product with concomitant removal of four hydrogen atoms. Interestingly, oxidation of procyanidin B1 occurs only in the presence of catechin or epicatechin and an additional product with an 864 Da molecular mass. In addition, procyanidin B1 is identified as a peroxidase substrate for the first time. Hindawi Publishing Corporation 2013 2013-10-24 /pmc/articles/PMC3821912/ /pubmed/24250715 http://dx.doi.org/10.1155/2013/412851 Text en Copyright © 2013 Yu-Ching Liu et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Liu, Yu-Ching Chen, Chao-Jung Lee, Miau-Rong Li, Mi Hsieh, Wen-Tsong Chung, Jing-Gung Ho, Heng-Chien
spellingShingle	Liu, Yu-Ching Chen, Chao-Jung Lee, Miau-Rong Li, Mi Hsieh, Wen-Tsong Chung, Jing-Gung Ho, Heng-Chien Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates
author_facet	Liu, Yu-Ching Chen, Chao-Jung Lee, Miau-Rong Li, Mi Hsieh, Wen-Tsong Chung, Jing-Gung Ho, Heng-Chien
author_sort	Liu, Yu-Ching
title	Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates
title_short	Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates
title_full	Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates
title_fullStr	Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates
title_full_unstemmed	Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates
title_sort	peroxidase as the major protein constituent in areca nut and identification of its natural substrates
description	Numerous reports illustrate the diverse effects of chewing the areca nut, most of which are harmful and have been shown to be associated with oral cancer. Nearly all of the studies are focused on the extract and/or low molecular weight ingredients in the areca nut. The purpose of this report is to identify the major protein component in the areca nut. After ammonium sulfate fractionation, the concentrated areca nut extract is subjected to DEAE-cellulose chromatography. A colored protein is eluted at low NaCl concentration and the apparently homogeneous eluent represents the major protein component compared to the areca nut extract. The colored protein shares partial sequence identity with the royal palm tree peroxidase and its peroxidase activity is confirmed using an established assay. In the study, the natural substrates of areca nut peroxidase are identified as catechin, epicatechin, and procyanidin B1. The two former substrates are similarly oxidized to form a 576 Da product with concomitant removal of four hydrogen atoms. Interestingly, oxidation of procyanidin B1 occurs only in the presence of catechin or epicatechin and an additional product with an 864 Da molecular mass. In addition, procyanidin B1 is identified as a peroxidase substrate for the first time.
publisher	Hindawi Publishing Corporation
publishDate	2013
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3821912/
_version_	1612024885008138240

Peroxidase as the Major Protein Constituent in Areca Nut and Identification of Its Natural Substrates

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