2023/05/19 by Rushit J. Shukla, Rushit Shukla, Satya P. Singh
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · #Enzyme Catalysis and Immobilization #Enzyme Production and Characterization #Phytase and its Applications
paper · doi:10.1002/star.202200254
openalex publication_date 2023/05/19 · crossref created 2023/05/19 · crossref issued 2023/06/22 · crossref published 2023/06/22 · crossref published-online 2023/06/22 · crossref published-print 2023/09/01 · crossref deposited 2023/09/12 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/03 · crossref indexed 2026/08/03
Abstract A thermophilic amylase produced by a newly isolated Geobacillus thermoleovorans TTIO4 from a hot spring in India is investigated. The isolate TTIO4 optimally produces extracellular amylase at 55 °C, pH 7, and 24 h of growth. The amylase is purified by 42 fold with a yield of 9.7%. The enzyme has a molecular weight of 40 kDa. The purified amylase catalyzes the reaction optimally at 60 °C and pH 7. Besides, it displays maximum thermal stability at 50 °C for 18 h. While the catalyst is improved by Ca +2 , it is wholly inhibited by Hg +2 . Furthermore, the chelators, inhibitors and solvents adversely affect the enzyme activity. The amylase is stabilized by SDS, while other surfactants negatively affect the enzyme. K m , V max , K cat , and K cat / K m of the amylase are 0.26 mg mL −1 , 192.3 µg mL −1 min −1 , 1.92 s −1 , and 7.383 s −1 mg −1 , respectively. The deactivation constant, half‐life, and change in Gibb's free energy, enthalpy, and entropy are determined at 50–70 °C, which supports the thermal stability and substrate affinity of the amylase. The washing quality of commercial detergents is distinctly enhanced when supplemented with this enzyme. Therefore, this amylase possesses significant thermal and surfactant stability has significant commercial potential.