Emochone, RY, Shaibu, C, Abah, MA, Mgbede, T, Ekele, JU, Ahmed, MU, Mohammed, RI, Iheanacho, C, Auta, FB, Saad, A, Anih, DC and Tibile, ST (2023) Isolation, Partial Purification and Characterization of Proteases from Aspergillus niger under Solid-State Fermentation. Asian Journal of Research in Biosciences, 5 (1). pp. 27-34.

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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 50 o C 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.

Item Type:	Article
Subjects:	G Geography. Anthropology. Recreation > GE Environmental Sciences Q Science > QH Natural history > QH301 Biology
Divisions:	Biological & Environmental Sciences (from Sep 19)
Publisher:	Global Press Hub.
SWORD Depositor:	A Symplectic
Date Deposited:	12 Feb 2024 09:29
Last Modified:	12 Feb 2024 09:31
URI:	https://researchonline.ljmu.ac.uk/id/eprint/22546

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