Cargando…

Pectin Methylesterase of Datura species, purification, and characterization from Datura stramoniumand its application

Pectin methylesterases (PME; EC 3.1.1.11) involved in de-esterification of pectin and have applicability in food, textiles, wines, pulp, and paper industries. In the present study, we compared PME activity of different parts of 3 Datura species and found that fruit coat showed maximum PME activity f...

Descripción completa

Detalles Bibliográficos
Autores principales: Dixit, Sameer, Upadhyay, Santosh Kumar, Singh, Harpal, Pandey, Bindu, Chandrashekar, Krishnappa, Verma, Praveen Chandra
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4091111/
https://www.ncbi.nlm.nih.gov/pubmed/23887498
http://dx.doi.org/10.4161/psb.25681
_version_ 1782480738578333696
author Dixit, Sameer
Upadhyay, Santosh Kumar
Singh, Harpal
Pandey, Bindu
Chandrashekar, Krishnappa
Verma, Praveen Chandra
author_facet Dixit, Sameer
Upadhyay, Santosh Kumar
Singh, Harpal
Pandey, Bindu
Chandrashekar, Krishnappa
Verma, Praveen Chandra
author_sort Dixit, Sameer
collection PubMed
description Pectin methylesterases (PME; EC 3.1.1.11) involved in de-esterification of pectin and have applicability in food, textiles, wines, pulp, and paper industries. In the present study, we compared PME activity of different parts of 3 Datura species and found that fruit coat showed maximum PME activity followed by leaf and seed. PME from leaves of D. stramonium (DsPME) was purified and characterized. DsPME showed optimum activity at 60 °C and pH 9 in the presence of 0.3 M NaCl. DsPME was stable at 70 °C and retained more than 40% activity after 60 min of incubation. However, enzyme activity completely abolished at 80 after 5 min of incubation. It follows Michaelis-Menten enzyme kinetics. Km and Vmax with citrus pectin were 0.008 mg/ml and 16.96 µmol/min, respectively. DsPME in combination with polygalactourenase (PGA) increased the clarity of orange, apple, pomegranate and pineapple juices by 2.9, 2.6, 2.3, and 3.6 fold, respectively in comparison to PGA alone. Due to very high de-esterification activity, easy denaturation and significant efficacy in incrementing clarification of fruit juice makes DsPME useful for industrial application.
format Online
Article
Text
id pubmed-4091111
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher Landes Bioscience
record_format MEDLINE/PubMed
spelling pubmed-40911112014-07-18 Pectin Methylesterase of Datura species, purification, and characterization from Datura stramoniumand its application Dixit, Sameer Upadhyay, Santosh Kumar Singh, Harpal Pandey, Bindu Chandrashekar, Krishnappa Verma, Praveen Chandra Plant Signal Behav Research Paper Pectin methylesterases (PME; EC 3.1.1.11) involved in de-esterification of pectin and have applicability in food, textiles, wines, pulp, and paper industries. In the present study, we compared PME activity of different parts of 3 Datura species and found that fruit coat showed maximum PME activity followed by leaf and seed. PME from leaves of D. stramonium (DsPME) was purified and characterized. DsPME showed optimum activity at 60 °C and pH 9 in the presence of 0.3 M NaCl. DsPME was stable at 70 °C and retained more than 40% activity after 60 min of incubation. However, enzyme activity completely abolished at 80 after 5 min of incubation. It follows Michaelis-Menten enzyme kinetics. Km and Vmax with citrus pectin were 0.008 mg/ml and 16.96 µmol/min, respectively. DsPME in combination with polygalactourenase (PGA) increased the clarity of orange, apple, pomegranate and pineapple juices by 2.9, 2.6, 2.3, and 3.6 fold, respectively in comparison to PGA alone. Due to very high de-esterification activity, easy denaturation and significant efficacy in incrementing clarification of fruit juice makes DsPME useful for industrial application. Landes Bioscience 2013-07-23 /pmc/articles/PMC4091111/ /pubmed/23887498 http://dx.doi.org/10.4161/psb.25681 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Research Paper
Dixit, Sameer
Upadhyay, Santosh Kumar
Singh, Harpal
Pandey, Bindu
Chandrashekar, Krishnappa
Verma, Praveen Chandra
Pectin Methylesterase of Datura species, purification, and characterization from Datura stramoniumand its application
title Pectin Methylesterase of Datura species, purification, and characterization from Datura stramoniumand its application
title_full Pectin Methylesterase of Datura species, purification, and characterization from Datura stramoniumand its application
title_fullStr Pectin Methylesterase of Datura species, purification, and characterization from Datura stramoniumand its application
title_full_unstemmed Pectin Methylesterase of Datura species, purification, and characterization from Datura stramoniumand its application
title_short Pectin Methylesterase of Datura species, purification, and characterization from Datura stramoniumand its application
title_sort pectin methylesterase of datura species, purification, and characterization from datura stramoniumand its application
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4091111/
https://www.ncbi.nlm.nih.gov/pubmed/23887498
http://dx.doi.org/10.4161/psb.25681
work_keys_str_mv AT dixitsameer pectinmethylesteraseofdaturaspeciespurificationandcharacterizationfromdaturastramoniumanditsapplication
AT upadhyaysantoshkumar pectinmethylesteraseofdaturaspeciespurificationandcharacterizationfromdaturastramoniumanditsapplication
AT singhharpal pectinmethylesteraseofdaturaspeciespurificationandcharacterizationfromdaturastramoniumanditsapplication
AT pandeybindu pectinmethylesteraseofdaturaspeciespurificationandcharacterizationfromdaturastramoniumanditsapplication
AT chandrashekarkrishnappa pectinmethylesteraseofdaturaspeciespurificationandcharacterizationfromdaturastramoniumanditsapplication
AT vermapraveenchandra pectinmethylesteraseofdaturaspeciespurificationandcharacterizationfromdaturastramoniumanditsapplication