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Partial Purification and Characterization of Exo-Polygalacturonase Produced by Penicillium oxalicum AUMC 4153
Pectinase enzymes are important industrial enzymes having considerable applications in several industries, especially in food processing. Pectinases contribute 25% of global food enzyme sales. Therefore, the demand for a commercial enzyme with desirable characteristics and low production costs has b...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8876663/ https://www.ncbi.nlm.nih.gov/pubmed/35207571 http://dx.doi.org/10.3390/life12020284 |
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author | Almowallad, Shamsan A. Alshammari, Ghedeir M. Alsayadi, Muneer M. Aljafer, Naofel Al-Sanea, Ekram A. Yahya, Mohammed Abdo Al-Harbi, Laila Naif |
author_facet | Almowallad, Shamsan A. Alshammari, Ghedeir M. Alsayadi, Muneer M. Aljafer, Naofel Al-Sanea, Ekram A. Yahya, Mohammed Abdo Al-Harbi, Laila Naif |
author_sort | Almowallad, Shamsan A. |
collection | PubMed |
description | Pectinase enzymes are important industrial enzymes having considerable applications in several industries, especially in food processing. Pectinases contribute 25% of global food enzyme sales. Therefore, the demand for a commercial enzyme with desirable characteristics and low production costs has become one of the great targets. Hence, this study aims to produce exo-polygalacturonase (exo-PG) using local fungal isolate Penicillium oxalicum AUMC 4153 by utilizing sugar beet manufacturing waste (sugar beet pulp) as a sole raw carbon source under shaken submerged fermentation, which is purified and characterized to optimize enzyme biochemical properties for industrial application. The purity of the obtained exo-PG was increased by about 28-fold, and the final enzyme yield was 57%. The partially purified enzyme was active at a broad range of temperatures (30–60 °C). The optimum temperature and pH for the purified exo-PG activity were 50 °C and pH 5. The enzyme was stable at a range of pH 3 to 6 and temperature 30–50 °C for 210 min. The values for K(m) and V(max) were 0.67 mg/mL, with polygalacturonic acid as substrate and 6.13 µmole galacturonic acid/min/mg protein, respectively. It can be concluded that purified exo-PG production by P. oxalicum grown on sugar beet waste is a promising effective method for useful applications. |
format | Online Article Text |
id | pubmed-8876663 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88766632022-02-26 Partial Purification and Characterization of Exo-Polygalacturonase Produced by Penicillium oxalicum AUMC 4153 Almowallad, Shamsan A. Alshammari, Ghedeir M. Alsayadi, Muneer M. Aljafer, Naofel Al-Sanea, Ekram A. Yahya, Mohammed Abdo Al-Harbi, Laila Naif Life (Basel) Article Pectinase enzymes are important industrial enzymes having considerable applications in several industries, especially in food processing. Pectinases contribute 25% of global food enzyme sales. Therefore, the demand for a commercial enzyme with desirable characteristics and low production costs has become one of the great targets. Hence, this study aims to produce exo-polygalacturonase (exo-PG) using local fungal isolate Penicillium oxalicum AUMC 4153 by utilizing sugar beet manufacturing waste (sugar beet pulp) as a sole raw carbon source under shaken submerged fermentation, which is purified and characterized to optimize enzyme biochemical properties for industrial application. The purity of the obtained exo-PG was increased by about 28-fold, and the final enzyme yield was 57%. The partially purified enzyme was active at a broad range of temperatures (30–60 °C). The optimum temperature and pH for the purified exo-PG activity were 50 °C and pH 5. The enzyme was stable at a range of pH 3 to 6 and temperature 30–50 °C for 210 min. The values for K(m) and V(max) were 0.67 mg/mL, with polygalacturonic acid as substrate and 6.13 µmole galacturonic acid/min/mg protein, respectively. It can be concluded that purified exo-PG production by P. oxalicum grown on sugar beet waste is a promising effective method for useful applications. MDPI 2022-02-14 /pmc/articles/PMC8876663/ /pubmed/35207571 http://dx.doi.org/10.3390/life12020284 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Almowallad, Shamsan A. Alshammari, Ghedeir M. Alsayadi, Muneer M. Aljafer, Naofel Al-Sanea, Ekram A. Yahya, Mohammed Abdo Al-Harbi, Laila Naif Partial Purification and Characterization of Exo-Polygalacturonase Produced by Penicillium oxalicum AUMC 4153 |
title | Partial Purification and Characterization of Exo-Polygalacturonase Produced by Penicillium oxalicum AUMC 4153 |
title_full | Partial Purification and Characterization of Exo-Polygalacturonase Produced by Penicillium oxalicum AUMC 4153 |
title_fullStr | Partial Purification and Characterization of Exo-Polygalacturonase Produced by Penicillium oxalicum AUMC 4153 |
title_full_unstemmed | Partial Purification and Characterization of Exo-Polygalacturonase Produced by Penicillium oxalicum AUMC 4153 |
title_short | Partial Purification and Characterization of Exo-Polygalacturonase Produced by Penicillium oxalicum AUMC 4153 |
title_sort | partial purification and characterization of exo-polygalacturonase produced by penicillium oxalicum aumc 4153 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8876663/ https://www.ncbi.nlm.nih.gov/pubmed/35207571 http://dx.doi.org/10.3390/life12020284 |
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