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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2013
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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 |
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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 |
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