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Hyperthermophilic archaea are a group of extremophiles thriving at temperatures above 80°C, often in hydrothermal vents and volcanic soils where conditions surpass the boiling point of water. At such temperatures, proteins, membranes, and DNA in most organisms degrade, but hyperthermophiles have evolved remarkable adaptations to maintain stability and function.Unique Cellular FeaturesHyperthermophilic membranes are composed of a monolayer of biphytanyl tetraether lipids, which resist...
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Crenarchaeota, a prominent phylum of Archaea, is remarkable for its ability to thrive in extreme environments characterized by high temperatures and acidity. These microorganisms inhabit sulfuric hot springs, volcanic systems, and submarine hydrothermal vents, where temperatures often exceed 100°C. The unique adaptations of Crenarchaeota not only allow survival under such extreme conditions but also provide insights into the mechanisms of life in primordial Earth-like...
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Domain Bacteria includes some unique hyperthermophilic species. They exhibit remarkable adaptations that enable survival in extreme environments.Thermotoga species are rod-shaped, gram-negative, non-sporulating hyperthermophiles that form a sheath-like envelope called a toga. They ferment sugars or starch, producing lactate, acetate, CO₂, and H₂, and can also grow via anaerobic respiration using H₂ and ferric iron. Found in hot springs and hydrothermal vents, over 20% of their...
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Amylases from thermophilic bacteria: structure and function relationship.

Bhavtosh A Kikani1,2, Satya P Singh1

  • 1UGC-CAS Department of Biosciences, Saurashtra University, Rajkot, India.

Critical Reviews in Biotechnology
|August 23, 2021
PubMed
Summary

Thermally stable amylases, crucial for industry, are reviewed focusing on structural traits and enhanced production via heterologous expression. Protein engineering and immobilization on nanomaterials improve enzyme stability and reusability for commercial use.

Keywords:
Thermostable α-amylasesenzyme immobilizationheterologous expressionmetagenomicsprotein engineeringstructural stability

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Area of Science:

  • Biochemistry and Biotechnology
  • Enzyme Engineering
  • Microbial Biotechnology

Background:

  • Amylases are enzymes that break down starch into smaller glucose units.
  • Thermally stable amylases represent a significant portion (25%) of the enzyme market.
  • Understanding the structural attributes of amylases from thermophilic bacteria is key to their industrial application.

Purpose of the Study:

  • To review the structural characteristics of alpha-amylases from thermophilic bacteria.
  • To discuss methods for enhancing amylase production and utility for commercial applications.
  • To explore novel amylases for future industrial use.

Main Methods:

  • Review of existing literature on thermophilic bacterial amylases.
  • Detailed discussion on heterologous expression of amylases.
  • Analysis of protein engineering and enzyme immobilization techniques, including on nanomaterials.

Main Results:

  • Structural attributes of thermophilic alpha-amylases are highlighted.
  • Heterologous expression provides a viable route for amylase production.
  • Immobilization on nanomaterials significantly enhances enzyme stability and reusability.

Conclusions:

  • Protein engineering and immobilization are effective strategies for commercializing amylases.
  • Nanomaterial-based immobilization offers superior stability and reusability.
  • Function-based metagenomics is a promising approach for discovering novel amylases.