Amylases from thermophilic bacteria: structure and function relationship

Abstract

Amylases hydrolyze starch to diverse products including dextrins and progressively smaller polymers of glucose units. Thermally stable amylases account for nearly 25% of the enzyme market. This review highlights the structural attributes of the α-amylases from thermophilic bacteria. Heterologous expression of amylases in suitable hosts is discussed in detail. Further, specific value maximization approaches, such as protein engineering and immobilization of the amylases are discussed in order to improve its suitability for varied applications on a commercial scale. The review also takes into account of the immobilization of the amylases on nanomaterials to increase the stability and reusability of the enzymes. The function-based metagenomics would provide opportunities for searching amylases with novel characteristics. The review is expected to explore novel amylases for future potential applications.

Keywords:

• Thermostable α-amylases
• structural stability
• enzyme immobilization
• protein engineering
• metagenomics
• heterologous expression

Disclosure statement

The authors report no declarations of interest.

Additional information

Funding

The work included in this review from the author’s laboratory at the Saurashtra University was supported under the University Grants Commission (UGC)-CAS Program, DST-FIST, DBT-Multi-Intuitional Project, MoES (Government of India) Net Working Project, and the Saurashtra University. SPS acknowledges DST-SERB International Travel Support to present his work in Kyoto, Japan. SPS also acknowledge award of UGC BSR Faculty Fellowship. BAK acknowledges DST-SERB, 2012, 2017 for the International Travel Support to present his research in the “Extremophiles-2012” and “FEMS-2017”, held in Seville, Spain and Valencia, Spain, respectively. BAK also acknowledges the award of the CSIR-Direct SRF (Government of India).