Enhanced Bacterial α-Amylase Production Using Mutant Strains Through Submerged Fermentation
Enhanced Bacterial α-Amylase Production Using Mutant Strains Through Submerged Fermentation
Muhammad Adeel Farooq1, Shaukat Ali1*, Ali Hassan1, Rida Sulayman1, Muhammad Ahsan Kaleem2, Hafsa Shahzad1, Muhammad Summer1, Arooj Latif1, Tahreem Tanveer1
ABSTRACT
The imperative enzyme alpha-amylase is used in various commercial and research applications. Due to the high market demand for α-amylase, the production of this enzyme was increased in the current study employing a mutation in wild strains. To reduce costs, less expensive agro-wastes were used, such as soybean meal, wheat bran, apple peels, rice husk, and cucumber peels. The mutant strains of Bacillus subtilis (BSAA-5 to BSAA-40) and Bacillus licheniformis (BLAA-5 to BLAA-40) were prepared by exposure to UV radiation for 5 to 40 min to synthesize α-amylase via submerged fermentation. Then the crude α-amylase synthesized by these mutant strains was optimized and partially characterized. In contrast to wild and all other mutant strain BSAA-25 and BLAA-25 strains showed the optimum production of α-amylase 331.4±6.9 U/mL and 310.8±11.3 U/mL, respectively, at 37±0.5°C and pH 7.0±0.2 for 48 h on wheat bran-based broth. BSAA-25 demonstrated maximum biosynthesis of α-amylase as compared to BLAA-25. Optimum α-amylase activity was measured at 40±0.5°C, pH 7.0±0.2 and 1% starch solution by BSAA-25 (338.6±11.0 U/mL) and BLAA-25 (326.8±6.4 U/mL). A considerable increase was seen in the biosynthesis of α-amylase from mutant strains of B. subtilis and B. licheniformis using agro-waste as substrate.
Novelty Statement | This scientific study presents an innovative strategy for increasing α-amylase production through the mutation and use of non-toxic agro-wastes such as soybean meal, wheat bran, apple peels, rice husk, and cucumber peels. The potential application of this approach contributes to the advancements in the fields of industrial biotechnology, and bioengineering.
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June 2023
Vol.38, Iss. 1, Pages 01-135
