Engineering Microbial Strains and Enzymes for Enhanced Productivity

Published: Jan. 1, 2025

Language: Английский

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Heterologous Expression and Biochemical Characterization of a New α-Amylase from Nocardiopsis aegyptia HDN19-252 of Antarctic Animal Origin

Marine Drugs, Journal Year: 2025, Volume and Issue: 23(4), P. 159 - 159

Published: April 4, 2025

α-Amylases, catalyzing starch degradation, serve as vital biocatalysts in industrial and pharmaceutical applications. This study identified a new α-amylase, Alphaz, from Nocardiopsis aegyptia HDN19-252 of Antarctic animal origin, achieving heterologous expression Escherichia coli. Phylogenetic analysis confirmed its classification into the GH13_5 subfamily glycoside hydrolases. Recombinant Alphaz exhibited optimal activity at 40 °C/pH 8.0 while maintaining stability across 0–30 °C pH 6.6–9.6. Its distinctive halotolerant properties included full retention 0.6 M NaCl >60% efficiency salt-free conditions. The enzyme exhibits tolerance to K+, Ca2+, Fe³+ demonstrating specific inhibition by Cu2+/Zn2+. With heterologously validated functional properties, emerges programmable enzymatic tool offering advantages sustained-release formulation quality control, targeted prodrug modification, precision medicine applications, thereby enabling sustainable biomanufacturing solutions that harmonize process reliability with environmental compatibility.

Language: Английский

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Optimization of thermostable amylolytic enzyme production from Bacillus cereus isolated from a recreational warm spring via Box Behnken design and response surface methodology

Microbial Cell Factories, Journal Year: 2025, Volume and Issue: 24(1)

Published: April 19, 2025

This study aimed to find a source for local amylase-producing microbes. Sixteen isolates were obtained from the water samples warm spring and characterized based on morphological biochemical tests. The 16S rRNA molecular identification technique confirmed most potent isolate as Bacillus cereus. thermophilic property of bacterium demonstrated that it could withstand temperatures up 80 °C. One-factor-at-a-time (OFAT) Box Behnken Design (BBD) coupled with response surface methodology (RSM) optimization techniques used improve amylase production. OFAT established optimal physical parameter conditions starch concentration 5% w/v, inoculum volume 2% v/v, pH 8, incubation temperature 45 °C, 48 h incubation, leading activity 172.6 U/mL by isolated B. A quadratic mathematical model coefficient determination (R2) 0.9957 was production process. Enhanced 196.02 achieved BBD-RSM under growth 7, time h, substrate w/v starch, at 1.2-fold increase compared method. cereus strain mildly potential synthesizing amylolytic enzymes characteristics beneficial commercial utilization.

Language: Английский

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Optimization and purification of a novel calcium-independent thermostable, α-amylase produced by Bacillus licheniformis UDS-5

World Journal of Microbiology and Biotechnology, Journal Year: 2024, Volume and Issue: 40(12)

Published: Nov. 19, 2024

Language: Английский

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