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Production and Partial Characterization of α-Amylase Enzyme from Bacillus sp. BCC 01-50 and Potential Applications
Amylase is an industrially important enzyme and applied in many industrial processes such as saccharification of starchy materials, food, pharmaceutical, detergent, and textile industries. This research work deals with the optimization of fermentation conditions for α-amylase production from thermop...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5267059/ https://www.ncbi.nlm.nih.gov/pubmed/28168200 http://dx.doi.org/10.1155/2017/9173040 |
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author | Simair, Altaf Ahmed Qureshi, Abdul Sattar Khushk, Imrana Ali, Chaudhry Haider Lashari, Safia Bhutto, Muhammad Aqeel Mangrio, Ghulam Sughra Lu, Changrui |
author_facet | Simair, Altaf Ahmed Qureshi, Abdul Sattar Khushk, Imrana Ali, Chaudhry Haider Lashari, Safia Bhutto, Muhammad Aqeel Mangrio, Ghulam Sughra Lu, Changrui |
author_sort | Simair, Altaf Ahmed |
collection | PubMed |
description | Amylase is an industrially important enzyme and applied in many industrial processes such as saccharification of starchy materials, food, pharmaceutical, detergent, and textile industries. This research work deals with the optimization of fermentation conditions for α-amylase production from thermophilic bacterial strain Bacillus sp. BCC 01-50 and characterization of crude amylase. The time profile of bacterial growth and amylase production was investigated in synthetic medium and maximum enzyme titer was observed after 60 h. In addition, effects of different carbon sources were tested as a substrate for amylase production and molasses was found to be the best. Various organic and inorganic compounds, potassium nitrate, ammonium chloride, sodium nitrate, urea, yeast extract, tryptone, beef extract, and peptone, were used and beef extract was found to be the best among the nitrogen sources used. Temperature, pH, agitation speed, and size of inoculum were also optimized. Highest enzyme activity was obtained when the strain was cultured in molasses medium for 60 h in shaking incubator (150 rpm) at 50°C and pH 8. Crude amylase showed maximal activity at pH 9 and 65°C. Enzyme remained stable in alkaline pH range 9-10 and 60–70°C. Crude amylase showed great potential for its application in detergent industry and saccharification of starchy materials. |
format | Online Article Text |
id | pubmed-5267059 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-52670592017-02-06 Production and Partial Characterization of α-Amylase Enzyme from Bacillus sp. BCC 01-50 and Potential Applications Simair, Altaf Ahmed Qureshi, Abdul Sattar Khushk, Imrana Ali, Chaudhry Haider Lashari, Safia Bhutto, Muhammad Aqeel Mangrio, Ghulam Sughra Lu, Changrui Biomed Res Int Research Article Amylase is an industrially important enzyme and applied in many industrial processes such as saccharification of starchy materials, food, pharmaceutical, detergent, and textile industries. This research work deals with the optimization of fermentation conditions for α-amylase production from thermophilic bacterial strain Bacillus sp. BCC 01-50 and characterization of crude amylase. The time profile of bacterial growth and amylase production was investigated in synthetic medium and maximum enzyme titer was observed after 60 h. In addition, effects of different carbon sources were tested as a substrate for amylase production and molasses was found to be the best. Various organic and inorganic compounds, potassium nitrate, ammonium chloride, sodium nitrate, urea, yeast extract, tryptone, beef extract, and peptone, were used and beef extract was found to be the best among the nitrogen sources used. Temperature, pH, agitation speed, and size of inoculum were also optimized. Highest enzyme activity was obtained when the strain was cultured in molasses medium for 60 h in shaking incubator (150 rpm) at 50°C and pH 8. Crude amylase showed maximal activity at pH 9 and 65°C. Enzyme remained stable in alkaline pH range 9-10 and 60–70°C. Crude amylase showed great potential for its application in detergent industry and saccharification of starchy materials. Hindawi Publishing Corporation 2017 2017-01-12 /pmc/articles/PMC5267059/ /pubmed/28168200 http://dx.doi.org/10.1155/2017/9173040 Text en Copyright © 2017 Altaf Ahmed Simair et al. https://creativecommons.org/licenses/by/4.0/ 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. |
spellingShingle | Research Article Simair, Altaf Ahmed Qureshi, Abdul Sattar Khushk, Imrana Ali, Chaudhry Haider Lashari, Safia Bhutto, Muhammad Aqeel Mangrio, Ghulam Sughra Lu, Changrui Production and Partial Characterization of α-Amylase Enzyme from Bacillus sp. BCC 01-50 and Potential Applications |
title | Production and Partial Characterization of α-Amylase Enzyme from Bacillus sp. BCC 01-50 and Potential Applications |
title_full | Production and Partial Characterization of α-Amylase Enzyme from Bacillus sp. BCC 01-50 and Potential Applications |
title_fullStr | Production and Partial Characterization of α-Amylase Enzyme from Bacillus sp. BCC 01-50 and Potential Applications |
title_full_unstemmed | Production and Partial Characterization of α-Amylase Enzyme from Bacillus sp. BCC 01-50 and Potential Applications |
title_short | Production and Partial Characterization of α-Amylase Enzyme from Bacillus sp. BCC 01-50 and Potential Applications |
title_sort | production and partial characterization of α-amylase enzyme from bacillus sp. bcc 01-50 and potential applications |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5267059/ https://www.ncbi.nlm.nih.gov/pubmed/28168200 http://dx.doi.org/10.1155/2017/9173040 |
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