A chimeric α-amylase engineered from Bacillus acidicola and Geobacillus thermoleovorans with improved thermostability and catalytic efficiency

Journal of Industrial Microbiology & Biotechnology
Deepak Parashar, T Satyanarayana

Abstract

The α-amylase (Ba-amy) of Bacillus acidicola was fused with DNA fragments encoding partial N- and C-terminal region of thermostable α-amylase gene of Geobacillus thermoleovorans (Gt-amy). The chimeric enzyme (Ba-Gt-amy) expressed in Escherichia coli displays marked increase in catalytic efficiency [K cat: 4 × 10(4) s(-1) and K cat/K m: 5 × 10(4) mL(-1) mg(-1) s(-1)] and higher thermostability than Ba-amy. The melting temperature (T m) of Ba-Gt-amy (73.8 °C) is also higher than Ba-amy (62 °C), and the CD spectrum analysis revealed the stability of the former, despite minor alteration in secondary structure. Langmuir-Hinshelwood kinetic analysis suggests that the adsorption of Ba-Gt-amy onto raw starch is more favourable than Ba-amy. Ba-Gt-amy is thus a suitable biocatalyst for raw starch saccharification at sub-gelatinization temperatures because of its acid stability, thermostability and Ca(2+) independence, and better than the other known bacterial acidic α-amylases.

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Citations

Aug 20, 2016·Applied Microbiology and Biotechnology·Haiquan YangFei Xu
Mar 16, 2017·Environmental Science and Pollution Research International·Himadri Bose, Tulasi Satyanarayana
Apr 7, 2017·Frontiers in Microbiology·Deepak Parashar, Tulasi Satyanarayana
May 29, 2021·PeerJ·Si Jie Lim, Siti Nurbaya Oslan
Aug 24, 2021·Critical Reviews in Biotechnology·Bhavtosh A Kikani, Satya P Singh

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