In this research, crude α-amylases associated with the spoilage of cassava (Manihot esculenta) tubers/ product (‘eba’) were biochemically characterized. They were isolated from five fungi: Aspergillus sp. CSA25, Aspergillus sp. CSA26, Aspergillus sp. CSA27, Aspergillus sp. CSA35 and Aspergillus sp. CSA38. The results of the analyses showed that the activities of α-amylase obtained from both sources (cassava tuber/ eba) were optimal at 45°C and pH 5.0. The maximum specific activity (Vmax) of the enzyme was found to be 10 U/mg protein, while its Michaelis-Menten constant (Km) was between 0.37 -1.25%w/v. The α-amylase is thermally stable for 1 - 2 h at optimum temperature and pH (45°C; pH 5.0). A broad range of substrate specificity was expressed by the enzyme for cassava starch-containing products (tapioca flour, garri flour, cassava flour, 1%, w/v); however, potato (Ipomoea batatas) starch, yam (Dioscorea rotundata) flour and cocoyam (Colocasia esculenta) flour were relatively minimally hydrolyzed by the crude α-amylases obtained from Aspergillus spp. that caused spoilage of cassava. Ethylenediamine tetraacetic acid (1 mM EDTA) and Mg2+ treatment had no significant (p > 0.05) effect on the activities of the amylase, but Na+, K+, Ca2+, Fe3+, thiourea and 5′,5′-dithiobis-2-nitrobenzoate (1 mM DTNB) enhanced its activities. The fungal α-amylases were most activated by K+ and had a salt tolerance of 1 - 2 M NaCl for 24 h. The fungal α-amylases reported in this study would find useful application in industries like food industry, detergent industry, paper industry, textile industry, pharmaceutical industry, etc where microbial α-amylases would be required for efficient and cost-effective hydrolysis of cassava starch, cassava flour and or its products.
Published in | Advances in Biochemistry (Volume 3, Issue 1) |
DOI | 10.11648/j.ab.20150301.14 |
Page(s) | 15-23 |
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. |
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Copyright © The Author(s), 2015. Published by Science Publishing Group |
Manihot esculenta (Cassava), Aspergillus spp., α-Amylase, Biochemical Characterization
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APA Style
Oghenetega Jonathan Avwioroko, Nyerhovwo John Tonukari, Samuel Ogheneovo Asagba. (2015). Biochemical Characterization of Crude α-Amylase of Aspergillus spp. Associated with the Spoilage of Cassava (Manihot esculenta) Tubers and Processed Products in Nigeria. Advances in Biochemistry, 3(1), 15-23. https://doi.org/10.11648/j.ab.20150301.14
ACS Style
Oghenetega Jonathan Avwioroko; Nyerhovwo John Tonukari; Samuel Ogheneovo Asagba. Biochemical Characterization of Crude α-Amylase of Aspergillus spp. Associated with the Spoilage of Cassava (Manihot esculenta) Tubers and Processed Products in Nigeria. Adv. Biochem. 2015, 3(1), 15-23. doi: 10.11648/j.ab.20150301.14
AMA Style
Oghenetega Jonathan Avwioroko, Nyerhovwo John Tonukari, Samuel Ogheneovo Asagba. Biochemical Characterization of Crude α-Amylase of Aspergillus spp. Associated with the Spoilage of Cassava (Manihot esculenta) Tubers and Processed Products in Nigeria. Adv Biochem. 2015;3(1):15-23. doi: 10.11648/j.ab.20150301.14
@article{10.11648/j.ab.20150301.14, author = {Oghenetega Jonathan Avwioroko and Nyerhovwo John Tonukari and Samuel Ogheneovo Asagba}, title = {Biochemical Characterization of Crude α-Amylase of Aspergillus spp. Associated with the Spoilage of Cassava (Manihot esculenta) Tubers and Processed Products in Nigeria}, journal = {Advances in Biochemistry}, volume = {3}, number = {1}, pages = {15-23}, doi = {10.11648/j.ab.20150301.14}, url = {https://doi.org/10.11648/j.ab.20150301.14}, eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20150301.14}, abstract = {In this research, crude α-amylases associated with the spoilage of cassava (Manihot esculenta) tubers/ product (‘eba’) were biochemically characterized. They were isolated from five fungi: Aspergillus sp. CSA25, Aspergillus sp. CSA26, Aspergillus sp. CSA27, Aspergillus sp. CSA35 and Aspergillus sp. CSA38. The results of the analyses showed that the activities of α-amylase obtained from both sources (cassava tuber/ eba) were optimal at 45°C and pH 5.0. The maximum specific activity (Vmax) of the enzyme was found to be 10 U/mg protein, while its Michaelis-Menten constant (Km) was between 0.37 -1.25%w/v. The α-amylase is thermally stable for 1 - 2 h at optimum temperature and pH (45°C; pH 5.0). A broad range of substrate specificity was expressed by the enzyme for cassava starch-containing products (tapioca flour, garri flour, cassava flour, 1%, w/v); however, potato (Ipomoea batatas) starch, yam (Dioscorea rotundata) flour and cocoyam (Colocasia esculenta) flour were relatively minimally hydrolyzed by the crude α-amylases obtained from Aspergillus spp. that caused spoilage of cassava. Ethylenediamine tetraacetic acid (1 mM EDTA) and Mg2+ treatment had no significant (p > 0.05) effect on the activities of the amylase, but Na+, K+, Ca2+, Fe3+, thiourea and 5′,5′-dithiobis-2-nitrobenzoate (1 mM DTNB) enhanced its activities. The fungal α-amylases were most activated by K+ and had a salt tolerance of 1 - 2 M NaCl for 24 h. The fungal α-amylases reported in this study would find useful application in industries like food industry, detergent industry, paper industry, textile industry, pharmaceutical industry, etc where microbial α-amylases would be required for efficient and cost-effective hydrolysis of cassava starch, cassava flour and or its products.}, year = {2015} }
TY - JOUR T1 - Biochemical Characterization of Crude α-Amylase of Aspergillus spp. Associated with the Spoilage of Cassava (Manihot esculenta) Tubers and Processed Products in Nigeria AU - Oghenetega Jonathan Avwioroko AU - Nyerhovwo John Tonukari AU - Samuel Ogheneovo Asagba Y1 - 2015/02/09 PY - 2015 N1 - https://doi.org/10.11648/j.ab.20150301.14 DO - 10.11648/j.ab.20150301.14 T2 - Advances in Biochemistry JF - Advances in Biochemistry JO - Advances in Biochemistry SP - 15 EP - 23 PB - Science Publishing Group SN - 2329-0862 UR - https://doi.org/10.11648/j.ab.20150301.14 AB - In this research, crude α-amylases associated with the spoilage of cassava (Manihot esculenta) tubers/ product (‘eba’) were biochemically characterized. They were isolated from five fungi: Aspergillus sp. CSA25, Aspergillus sp. CSA26, Aspergillus sp. CSA27, Aspergillus sp. CSA35 and Aspergillus sp. CSA38. The results of the analyses showed that the activities of α-amylase obtained from both sources (cassava tuber/ eba) were optimal at 45°C and pH 5.0. The maximum specific activity (Vmax) of the enzyme was found to be 10 U/mg protein, while its Michaelis-Menten constant (Km) was between 0.37 -1.25%w/v. The α-amylase is thermally stable for 1 - 2 h at optimum temperature and pH (45°C; pH 5.0). A broad range of substrate specificity was expressed by the enzyme for cassava starch-containing products (tapioca flour, garri flour, cassava flour, 1%, w/v); however, potato (Ipomoea batatas) starch, yam (Dioscorea rotundata) flour and cocoyam (Colocasia esculenta) flour were relatively minimally hydrolyzed by the crude α-amylases obtained from Aspergillus spp. that caused spoilage of cassava. Ethylenediamine tetraacetic acid (1 mM EDTA) and Mg2+ treatment had no significant (p > 0.05) effect on the activities of the amylase, but Na+, K+, Ca2+, Fe3+, thiourea and 5′,5′-dithiobis-2-nitrobenzoate (1 mM DTNB) enhanced its activities. The fungal α-amylases were most activated by K+ and had a salt tolerance of 1 - 2 M NaCl for 24 h. The fungal α-amylases reported in this study would find useful application in industries like food industry, detergent industry, paper industry, textile industry, pharmaceutical industry, etc where microbial α-amylases would be required for efficient and cost-effective hydrolysis of cassava starch, cassava flour and or its products. VL - 3 IS - 1 ER -