Isolation, Partial Purification and Characterization of Proteases from Aspergillus niger under Solid-State Fermentation

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Published: 2023-11-30

Page: 27-34


Emochone Roy Yohanna *

Department of Biochemistry, Faculty of Pure and Applied Sciences, Federal University Wukari, Taraba State, Nigeria.

Anih David Chinonso

Department of Biochemistry, Faculty of Pure and Applied Sciences, Federal University Wukari, Taraba State, Nigeria.

Saad Abdulkadir

Department of Biochemistry, Faculty of Pure and Applied Sciences, Kwara State Polytechnic. PMB 1375, Ilorin, Kwara State, Nigeria

Faith Beyaan Auta

Department of Microbiology, Faculty of Pure and Applied Sciences, Joseph Sarwuan Tarkaa University, Benue State, Nigeria.

Chinedu Christian Iheanacho

Department of Microbiology, Faculty of Pure and Applied Sciences, Federal University Wukari, Taraba State, Nigeria.

Rashida Ismail Mohammed

Department of Integrated Science, School of Sciences, College of Education and Legal Studies, Nguru, Yobe State, Nigeria.

Maryam Usman Ahmed

Department of Biochemistry, Faculty of Pure and Applied Sciences, Adamawa State University, Mubi, Nigeria.

Ekele Jiata Ugwah

Department of Sustainable Agriculture and Food Security, Newcastle University, NE1 7RU, UK.

Mgbede Timothy

Department of Biochemistry, Faculty of Pure and Applied Sciences, Federal University Wukari, Taraba State, Nigeria.

Moses Adondua Abah

Department of Biochemistry, Faculty of Pure and Applied Sciences, Federal University Wukari, Taraba State, Nigeria and Department of Medical Biochemistry, Faculty of Basic Medical Sciences, Federal University Wukari, Taraba State, Nigeria.

Christopher Shaibu

Department of Biochemistry, Faculty of Pure and Applied Sciences, Federal University Wukari, Taraba State, Nigeria.

Sojay Tryphosa Tibile

Department of Food Nutrition and Home Sciences, Faculty of Agriculture, Prince Abubakar Audu University, Anyigba, Kogi State, Nigeria.

*Author to whom correspondence should be addressed.


Abstract

Proteases are enzymes with highly specialized proteolytic functions. They are ubiquitous, being found in all living organisms, they are essential for cell growth and differentiation. Besides their physiological functions and roles in living organisms, they also show great importance in various industries. The shortage of plant and animal proteases to meet the present world demand of industrial enzymes has directed increased interest in microbial proteases. Several researchers have reported on protease production from various sources. However, little is known about protease production using A. niger under solid-state fermentation. This present investigation was carried out to isolate and screen fungi from soil samples for the production, optimization, and characterization of protease. A. niger was identified morphologically and screened for protease production. Soli-state fermentation was carried out and crude protease was harvested. The effect of pH on protease activity was assayed, and different temperatures were used to test for protease activity. Also, the kinetic parameters (Km and Vmax) of the crude enzyme were also determined. The results of this investigation revealed that the optimal pH and temperature of the enzyme were 8.0 and 40°C, respectively. The enzyme was found to be more stable at alkaline pH than acidic pH. It also retained 80% of its activity at 50oC for 60 minutes. Protease activity was revealed to be highest at substrate concentration 1.0 mM. All these data suggest that the selected strain of A. niger can significantly produce protease enzyme under solid-state fermentation.

Keywords: Tassel, Proteases, Wood, catalytic activity, Seeding,, substrate, epigeal germination, fermentation, Aspergillus niger


How to Cite

Yohanna, Emochone Roy, Anih David Chinonso, Saad Abdulkadir, Faith Beyaan Auta, Chinedu Christian Iheanacho, Rashida Ismail Mohammed, Maryam Usman Ahmed, et al. 2023. “Isolation, Partial Purification and Characterization of Proteases from Aspergillus Niger under Solid-State Fermentation”. Asian Journal of Research in Biosciences 2023 (5):27-34. https://journalbioscience.com/index.php/AJORIB/article/view/22.

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