Heterologous Expression and Biochemical Characterization of a New α-Amylase from <i>Nocardiopsis aegyptia</i> HDN19-252 of Antarctic Animal Origin
α-Amylases, catalyzing starch degradation, serve as vital biocatalysts in industrial and pharmaceutical applications. This study identified a new α-amylase, Alphaz, from <i>Nocardiopsis aegyptia</i> HDN19-252 of Antarctic animal origin, achieving heterologous expression in <i>Esche...
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| Main Authors: | , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-04-01
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| Series: | Marine Drugs |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1660-3397/23/4/159 |
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| Summary: | α-Amylases, catalyzing starch degradation, serve as vital biocatalysts in industrial and pharmaceutical applications. This study identified a new α-amylase, Alphaz, from <i>Nocardiopsis aegyptia</i> HDN19-252 of Antarctic animal origin, achieving heterologous expression in <i>Escherichia coli</i>. Phylogenetic analysis confirmed its classification into the GH13_5 subfamily of glycoside hydrolases. Recombinant Alphaz exhibited optimal activity at 40 °C/pH 8.0 while maintaining stability across 0–30 °C and pH 6.6–9.6. Its distinctive halotolerant properties included full activity retention in 0.6 M NaCl and >60% efficiency in salt-free conditions. The enzyme exhibits tolerance to K<sup>+</sup>, Ca<sup>2+</sup>, and Fe³<sup>+</sup> while demonstrating specific inhibition by Cu<sup>2+</sup>/Zn<sup>2+</sup>. With its heterologously validated functional properties, Alphaz emerges as a programmable enzymatic tool offering advantages in sustained-release formulation quality control, targeted prodrug modification, and precision medicine applications, thereby enabling sustainable biomanufacturing solutions that harmonize process reliability with environmental compatibility. |
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| ISSN: | 1660-3397 |