Protease was obtained from Aspergillus niger isolated from yam peels; a food waste, purified and characterized. Purification was achieved using ion exchange DEAE column and gel filtration (Sephadex G-200) chromatography. Effects of temperature; pH and production time on protease production were investigated. Also, physicochemical characteristics of the purified enzyme were investigated. The optimum production of protease was at temperature, pH and time of 37oC, 7.0 and 42 hrs respectively. The results showed that purified protease had more specific enzymatic activity than crude samples from Aspergillus Niger. whereas the specific activity of crude enzyme was 0.51 (U/mg), while the purified enzyme had an improved specific activity of 8.51 (U/mg).Optimum temperature and pH values of the purified protease were found to be 50°C and 10.0, respectively. pH stability of the enzyme ranged from 3.0- 12.0. At 3.0 and 10.0 it retained 70% and 60% of its activity after 5 hrs of incubation. Temperature stability ranged between 30oC and 90oC but most stable at 50oC retaining 94% of its activity after 1 h of incubation. The enzyme exhibited maximum activity on casein, among other protein substrates. EDTA, Cu2+, Fe2+, Mg 2+, and Ca2+ inhibited its activity while Na+ enhanced it. The enzyme was purified 16.60-fold, had a yield of 10.96 and the apparent molecular weight was 46.90 kDa. The study revealed that protease from A. niger can be exploited for protein conversion biotechnologies.
| Published in | International Journal of Nutrition and Food Sciences (Volume 4, Issue 2) |
| DOI | 10.11648/j.ijnfs.20150402.11 |
| Page(s) | 125-131 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2015. Published by Science Publishing Group |
Protease, Aspergillus Niger, Yam Peels, Fermentation, Purification, Characterisation
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APA Style
Oludumila Omolara Racheal, Abu Temitope Folagbade Ahmed, Enujiugha Victor Ndigwe, Sanni David Morakinyo. (2015). Extraction, Purification and Characterization of Protease from Aspergillus Niger Isolated from Yam Peels. International Journal of Nutrition and Food Sciences, 4(2), 125-131. https://doi.org/10.11648/j.ijnfs.20150402.11
ACS Style
Oludumila Omolara Racheal; Abu Temitope Folagbade Ahmed; Enujiugha Victor Ndigwe; Sanni David Morakinyo. Extraction, Purification and Characterization of Protease from Aspergillus Niger Isolated from Yam Peels. Int. J. Nutr. Food Sci. 2015, 4(2), 125-131. doi: 10.11648/j.ijnfs.20150402.11
AMA Style
Oludumila Omolara Racheal, Abu Temitope Folagbade Ahmed, Enujiugha Victor Ndigwe, Sanni David Morakinyo. Extraction, Purification and Characterization of Protease from Aspergillus Niger Isolated from Yam Peels. Int J Nutr Food Sci. 2015;4(2):125-131. doi: 10.11648/j.ijnfs.20150402.11
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Download@article{10.11648/j.ijnfs.20150402.11,
author = {Oludumila Omolara Racheal and Abu Temitope Folagbade Ahmed and Enujiugha Victor Ndigwe and Sanni David Morakinyo},
title = {Extraction, Purification and Characterization of Protease from Aspergillus Niger Isolated from Yam Peels},
journal = {International Journal of Nutrition and Food Sciences},
volume = {4},
number = {2},
pages = {125-131},
doi = {10.11648/j.ijnfs.20150402.11},
url = {https://doi.org/10.11648/j.ijnfs.20150402.11},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijnfs.20150402.11},
abstract = {Protease was obtained from Aspergillus niger isolated from yam peels; a food waste, purified and characterized. Purification was achieved using ion exchange DEAE column and gel filtration (Sephadex G-200) chromatography. Effects of temperature; pH and production time on protease production were investigated. Also, physicochemical characteristics of the purified enzyme were investigated. The optimum production of protease was at temperature, pH and time of 37oC, 7.0 and 42 hrs respectively. The results showed that purified protease had more specific enzymatic activity than crude samples from Aspergillus Niger. whereas the specific activity of crude enzyme was 0.51 (U/mg), while the purified enzyme had an improved specific activity of 8.51 (U/mg).Optimum temperature and pH values of the purified protease were found to be 50°C and 10.0, respectively. pH stability of the enzyme ranged from 3.0- 12.0. At 3.0 and 10.0 it retained 70% and 60% of its activity after 5 hrs of incubation. Temperature stability ranged between 30oC and 90oC but most stable at 50oC retaining 94% of its activity after 1 h of incubation. The enzyme exhibited maximum activity on casein, among other protein substrates. EDTA, Cu2+, Fe2+, Mg 2+, and Ca2+ inhibited its activity while Na+ enhanced it. The enzyme was purified 16.60-fold, had a yield of 10.96 and the apparent molecular weight was 46.90 kDa. The study revealed that protease from A. niger can be exploited for protein conversion biotechnologies.},
year = {2015}
}
TY - JOUR T1 - Extraction, Purification and Characterization of Protease from Aspergillus Niger Isolated from Yam Peels AU - Oludumila Omolara Racheal AU - Abu Temitope Folagbade Ahmed AU - Enujiugha Victor Ndigwe AU - Sanni David Morakinyo Y1 - 2015/02/16 PY - 2015 N1 - https://doi.org/10.11648/j.ijnfs.20150402.11 DO - 10.11648/j.ijnfs.20150402.11 T2 - International Journal of Nutrition and Food Sciences JF - International Journal of Nutrition and Food Sciences JO - International Journal of Nutrition and Food Sciences SP - 125 EP - 131 PB - Science Publishing Group SN - 2327-2716 UR - https://doi.org/10.11648/j.ijnfs.20150402.11 AB - Protease was obtained from Aspergillus niger isolated from yam peels; a food waste, purified and characterized. Purification was achieved using ion exchange DEAE column and gel filtration (Sephadex G-200) chromatography. Effects of temperature; pH and production time on protease production were investigated. Also, physicochemical characteristics of the purified enzyme were investigated. The optimum production of protease was at temperature, pH and time of 37oC, 7.0 and 42 hrs respectively. The results showed that purified protease had more specific enzymatic activity than crude samples from Aspergillus Niger. whereas the specific activity of crude enzyme was 0.51 (U/mg), while the purified enzyme had an improved specific activity of 8.51 (U/mg).Optimum temperature and pH values of the purified protease were found to be 50°C and 10.0, respectively. pH stability of the enzyme ranged from 3.0- 12.0. At 3.0 and 10.0 it retained 70% and 60% of its activity after 5 hrs of incubation. Temperature stability ranged between 30oC and 90oC but most stable at 50oC retaining 94% of its activity after 1 h of incubation. The enzyme exhibited maximum activity on casein, among other protein substrates. EDTA, Cu2+, Fe2+, Mg 2+, and Ca2+ inhibited its activity while Na+ enhanced it. The enzyme was purified 16.60-fold, had a yield of 10.96 and the apparent molecular weight was 46.90 kDa. The study revealed that protease from A. niger can be exploited for protein conversion biotechnologies. VL - 4 IS - 2 ER -
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