Optimization of Amylase Production in Three Fungal Species

F. E. Ekedegba *

Department of Plant Science & Biotechnology, University of Jos, Nigeria.

A. I. Ogbonna

Department of Plant Science & Biotechnology, University of Jos, Nigeria.

B. M. W. Nwibari

Department of Zoology & Environmental Biology, University of Calabar, Nigeria.

C. T. Okoye

Department of Integrated Plant Science, University of Georgia, Athens, GA, USA.

U. S. A. Ogbonna

Department of Applied Microbiology & Brewing, Nnamdi Azikiwe University, Awka, Nigeria.

I. A. Onyimba

Department of Science Laboratory Technology, University of Jos, Nigeria.

J. M. Madu

National Biotechnology Development Agency, Airport Road, Lugbe, Abuja, Nigeria.

A. I. Njoku

Department of Science Laboratory Technology, University of Jos, Nigeria.

*Author to whom correspondence should be addressed.


Aim: Amylase is an important enzyme that is employed in starch processing industries, used in the hydrolysis of polysaccharides such as starch into simple sugar constituents. In this study, we investigated the abilities of several isolated amylolytic soil fungi to produce amylase.

Materials and Methods: Soil samples collected from the botanical garden, Department of Plant Science and Biotechnology, University of Jos was serially diluted and screened for the presence of amylase producing fungi. Optimization studies was performed across different parameters; Incubation period (7 days), different temperatures (25-60°C), different pH (5-9), different starch concentration (0.2-2%), carbon source (sucrose, maltose, lactose).

Results: A total of 15 isolates belonging to 7 genera were isolated. Soil samples were analyzed for their ecological parameters. The plate assay showed that three species T. viride (62mm), P. citrinum (50.25mm), and A. niger (67mm) had the largest zones of clearance and highest amylolytic activity thus were selected for further studies. For submerged fermentation, optimum amylolytic activity was observed at 24 hours of incubation for all three species T. viride (7.92 IU/ml), P. citrinum (5.04 IU/ml), and A. niger (7.00 IU/ml). Maximum enzyme activity was observed at incubation temperature of 45°C (17.10 IU/ml) for T. viride, 50°C (33.60 IU/ml) for P. citrinum, and 50°C (14.30 IU/ml) for A. niger. The maximum enzyme activity was at pH 9 (20.40 IU/ml) for T. viride, pH 11 (18.50 IU/ml) for P. citrinum, and pH 7 (25.80 IU/ml) for A. niger. T. viride and P. citrinum recorded an optimum enzyme activity of 15.40 IU/ml and 13.20 IU/ml respectively when sucrose was used as a carbon source while A. niger recorded an optimum activity of 7.28 IU/ml when maltose was used. Starch concentration of 2% showed the highest enzyme activity of 16.52 IU/ml, 15.4 IU/ml and 14.00 IU/ml, for T. viride, A. niger and P. citrinum, respectively.

Conclusion: Trichoderma viride, Penicillium citrinum, and Aspergillus niger showed potential of producing amylase which is useful in the biodegradation of biological wastes.

Keywords: Amylase, Trichoderma viride, Penicillium citrinum, Aspergillus niger, Amylolytic activity, Soil fungi

How to Cite

Ekedegba, F. E., Ogbonna, A. I., Nwibari, B. M. W., Okoye, C. T., Ogbonna, U. S. A., Onyimba, I. A., Madu, J. M., & Njoku, A. I. (2022). Optimization of Amylase Production in Three Fungal Species. Asian Journal of Biochemistry, Genetics and Molecular Biology, 12(4), 1–9. https://doi.org/10.9734/ajbgmb/2022/v12i4266


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Akpan I. Bankjole MO, Adesermowo AM. Production of Amylase by Aspergillus niger in a cheap solid medium using rice bran and agricultural material. Tropical Science. 1999;39:77-79.

Jiby JM, Prem JV, Sajeshkuma NK, and Anjaly A. Amylase Production by Aspergillus niger through Submerged Fermentation using Starchy Food Products as Substrate. International Journal of Herbal Medicine. 2016; 4(6):34-40.

Buzzini P. and Martini A. Extracellular enzymatic activity profiles in yeast and yeast like strains isolated from tropical environments. Journal of Applied Microbiology 2002; 93:1020-1025.

Saranraj P, Stella D. Fungal Amylase: A Review. International journal of Microbiological Research. 2013; 4: 203-211.

Gupta A, Gupta VL, Modi DR, and Yadava LP. Production and characterization of α-amylase from Aspergillus niger. Biotechnology. 2008; 7:551-556.

Abu EA, Ado SA, James DB. Raw starch degrading amylase production by mixed culture of Aspergillus niger and Saccharomyces cerevisae grown on Sorghum pomace. African Journal of Biotechnology. 2005;4:785-790.

Swetha S, Dhanya G, Kesavan MN, Carlos RS, and Ashok P. α- Amylases from Microbial Sources- An Overview on Recent Developments. Food Technology Biotechnology. 2006;44: 173-184.

Okonkwoeje AI. The effect of Different Soil Samples in the Remediation of Crude Oil Polluted Nigerian Agricultural Soil M.Sc. Dissertation University of Jos; 2000.

Ogbonna CIC, and Pugh GJF. Nigerian Soil fungi, Nova Hedweigia. 1982; 36:795-808.

Domsch KH, Gams W, and Anderson TH. Compendium of Soil Fungi. 2nd Edition, IHW-Verlag, Eching, 2007.

Ogbonna CN, Nnaji OB, and Chioke OJ. Isolation of amylase and Cellulase producing Fungi from Decaying Tubers and Optimization of their Enzyme Production in Solid and Submerged Cultures. International Journal of Biotechnology and Food Science. 2018; 6: 9-17.

Toye E. Laboratory Production and Assay of Amylase by Fungi and Bacteria Manual. UW- Washington County. 1-7.

Soonmro IH, Yasmeen FK, Miandad Z, and Abdul HS. Isolation of Keratinophilic Fungi from Soil in Khairpur City, Sindh, Pakistan. Bangladesh Journal of Microbiology. 2007;24:79-80.

Lavelle P, and Spain AV. Soil Ecology, Chapter 3, Springer; 2005.

Obire O, Nwaubeta O. Effects of Refined Petroleum Hydrocarbon on soil Physicochemical and Bacteriological Characteristics. Journal of Applied Sciences and Environmental Management. 2002; 6(1):39-44.

Nahas E, Waldemarin MM. Control of Amylase Production and Growth Characteristics of Aspergillus ochraceus. Revista Latinoamericana de Microbiologia. 2002;44(1):5-10.

Duochaun LY Yijun P, Youliang S. Chongyao Z. Peijin and H. Yicum. Purification and properties of Thermostable Alpha Amylase from Thermophillic Fungus Thermomyces lanuginosus. Acta. Microbiology SIN. 1997;37:107-117.

Sun H, Zhao P, Ge X, Xia Y, Hao Z, Liu J, and Peng M. Recent Advances in Microbial Raw Starch Degrading Enzymes. Applied Biochemistry and Biotechnology. 2010; 160: 988-1003.

Ertan F, Yagar H, and Balkan B. Some Properties of Free and Immobilized α-Amylase from Penicillium griseofulvum by Solid State Fermentation. Preperative Biochemistry and Biotechnology. 2006; 36: 81-91.

Kubilay M, Öznur K, Burcu BAZ, and Halil BH. Purification and Characterization of α-Amylase Produced by Penicillium citrinum HBF62.African Journal of Biotechnology. 2010;9:7692-7701.

Sazzad M, and Sabita RR. Production and Partial Characterization of Extracellular α-Amylases by Trichoderma viride. Bangladesh Journal of Microbiology. 2008; 25: 99- 103.

Gupta R, Gigras P, Mohapatra H, Goswami VK, and Chauhan B. Microbial α-Amylases: A Biotechnological Perspective. Process. Biochemistry. 2003; 38: 1599-1616.

Nguyen QD, Rezessy-Szabó JB, and Hoschke Á. Optimization of Composition of Media for the Production of Amylolytic Enzymes by Thermomyces lanuginosus ATCC 34626. Food Technology and Biotechnology. 2000;38:229- 234.

Moreira FG, Lenartovicz V, Cristina GM, Ramos EP, and Peralta RM. The Use of α-Methyl-d-glucoside, a Synthetic Analogue of Maltose, as Inducer of Amylase by Aspergillus sp. in Solid-State and Submerged Fermentations. Brazilian Journal of Microbiology. 2001;3:15- 19.