Jul 2026· Journal of the College of Basic Education· 0 citations
TL;DR
Among the 20 isolates, one isolate was identified as Brevibacillus parabrevis PS12, representing the first report from Iraqi soil, which contributed to an increase in bacterial biomass which led to a rise in the specific activity of arginase.
Abstract
Soil-occupy Brevibacillus parabrevius PS12 species are known for their metabolically versatile and it is being discovered as source of natural enzymes valuable to industry. Arginase catalyzes the processing of L-arginine to L-ornithine and urea, it is the one that plays a significant role in nitrogen metabolism Finding novel bacterial strains from environmental sources that are capable of producing the arginase enzyme is crucial for expanding microbial resources for industrial and pharmaceutical use. Among the 20 isolates, one isolate was identified as Brevibacillus parabrevis PS12 (97% 16S rRNA similarity, GenBank accession no. (PX118439.1), representing the first report from Iraqi soil. Arginase activity reached 8.3 U/mg protein a peak in nutritional source with maltose as a arbone source and casein as a Nitrogen source, the physical parameters also effect on enzyme specific activity at 7.0 pH, 37°C, and 48 hours of incubation time with shaker incubator 150 rpm to ensure the homogeneity of all medium components and continuous aeration all these factors contributed to an increase in bacterial biomass which led to a rise in the specific activity of arginase.
L-Asparaginase is an important enzyme with therapeutic applications. Current commercial enzymes from E. coli and Erwinia chrysanthemi have limitations, such as high glutaminase activity, creating a need for more stable alternatives. This study aimed to isolate and optimize the production of L-Asparaginase from native, halotolerant Bacillus subtilis strains (DAR and D6A) isolated from central Iran, to find an alternative source for this therapeutically important enzyme. The enzyme was initially isolated using polyethylene glycol (PEG) precipitation. Key factors affecting enzyme production were screened using the Plackett-Burman design and subsequently optimized via the Box-Behnken response surface methodology. PEG precipitation at concentrations of 15-20% for PEG 4000/6000 and 10-15% for PEG 8000/10000 was most effective for initial enzyme separation, yielding specific activities of 4.8 U/mg and 5.2 U/mg for strains DAR and D6A, respectively. Optimization revealed that the most influential factors for maximum L-Asparaginase production were 17.6 g/L NaCl, 4.99 g/L KH2PO4, and 10 g/L asparagine for strain DAR, and 1.49 g/L glucose, 10 g/L NaCl, and 9.98 g/L asparagine for strain D6A. The isolated halotolerant B. subtilis strains are capable of producing L-Asparaginase. PEG precipitation is a suitable method for initial purification, and statistical optimization successfully identified the critical culture conditions to enhance enzyme yield significantly. These strains represent promising sources for the production of this clinically valuable enzyme.
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