Isolation and Characterization of Aeromonas taiwanensis Strain for Simultaneous Production of Cellulase, Amylase, Pectinase, and Protease Enzymes.

Supriya Gupta¹, Aiman Tanveer^1*, Shruti Dwivedi¹, Kanchan Yadav¹ , Vivek Kumar Morya² and Dinesh Yadav^1*

¹Department of Biotechnology, Deen Dayal Upadhyaya Gorakhpur University, Gorakhpur, (Uttar Pradesh)-India

²Department of Orthopedic Surgery, Dongtan Sacred Heart Hospital, School of Medicine, Hallym University, Dongtan, South Korea

Corresponding Author E-mail: dinesh_yad@rediffmail.com

DOI : http://dx.doi.org/10.13005/bbra/3254

ABSTRACT: A study was conducted to discover a novel microorganism capable of producing multiple enzymes with industrial applications. Bacterial isolates were screened from a soil sample collected from a wood-decaying area, and their ability to produce various enzymes of industrial significance was evaluated. Among the 100 screened bacterial isolates, the strain GCEL-BGb85 was identified as Aeromonas taiwanensis through 16s RNA sequencing. Further screening revealed that this microorganism could produce cellulase, pectinase, protease, and amylase enzymes. The strain was set up for enzyme production, and the enzyme activity levels for cellulase, amylase, pectinase, and protease were 0.071, 0.201, 0.202, and 0.152 U/ml, respectively. All four enzymes demonstrated optimal activity at 40°C with a distinct pH. The zymogram analysis confirmed the presence of these enzymes in the isolated bacterial strain. As all the enzymes isolated from this strain are industrially significant, the application of the cell-free extract containing all these enzymes was evaluated at a laboratory scale for its potential use in industrial applications. The enzyme cocktail demonstrated its utility in the retting of fibers, effectively removing blood and egg yolk stains and extracting fruit juices and oil. The enzyme extract was also found to be useful in sustainable waste management.

KEYWORDS: Aeromonas Taiwanensis; Industrial Enzymes; Hydrolytic Enzymes; Saprotroph

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