Related Experiment Video
Updated: Aug 1, 2026
20:28
A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments
Published on: October 2, 2012
Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon
Yuji Hotta1, Satoshi Ezaki, Haruyuki Atomi
1Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Yoshida-Honmachi, Sakyo-ku, Kyoto 606-8501, Japan.
Applied and Environmental Microbiology
|July 31, 2002
Summary
A thermostable esterase from Pyrobaculum calidifontis VA1 was identified and characterized. This enzyme exhibits high activity and stability at extreme temperatures and in organic solvents, showing potential for industrial applications.
Area of Science:
- Biochemistry
- Enzymology
- Extremophile Biology
Background:
- Hyperthermophilic archaea, such as Pyrobaculum calidifontis VA1, are sources of robust enzymes.
- Esterases are crucial biocatalysts with diverse industrial applications.
- Thermostable enzymes are highly sought after for processes requiring high temperatures or harsh conditions.
Purpose of the Study:
- To isolate and characterize a novel thermostable esterase from Pyrobaculum calidifontis VA1.
- To investigate the enzyme's biochemical properties, including substrate specificity and stability.
- To assess the potential industrial applicability of the identified esterase.
Main Methods:
- Isolation and gene sequencing of the esterase (est(Pc)) from P. calidifontis VA1.
- Recombinant expression and purification of the esterase (Est).
- Enzyme activity assays at various temperatures and substrate concentrations.
- Stability tests in the presence of organic solvents and heat.
Main Results:
- The est(Pc) gene encodes a 313-amino acid esterase (Est) with high identity to mammalian hormone-sensitive lipases.
- Est demonstrated high catalytic activity at both high (90°C) and ambient (30°C) temperatures.
- The enzyme exhibited exceptional thermostability and stability in 80% organic solvents, with unique activity towards tertiary alcohol esters.
Conclusions:
- Est of P. calidifontis is a novel, highly stable esterase with broad substrate specificity.
- Its remarkable stability and unique activity profile suggest significant potential for industrial biocatalysis.
- This enzyme represents a valuable tool for applications requiring robust lipolytic activity under extreme conditions.
Related Concept Videos
01:29Biosynthesis of Lipids
Microbial membranes exhibit remarkable diversity in lipid composition, reflecting evolutionary adaptations to various environmental conditions. The three domains of life—Bacteria, Archaea, and Eukarya—synthesize membrane lipids through distinct biosynthetic pathways, leading to fundamental structural differences that impact membrane stability, function, and adaptability.Fatty Acid-Based Lipids in Bacteria and EukaryaBacteria and eukaryotes share a common fatty acid biosynthesis pathway, which...
01:21Hyperthermophilic Bacteria
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 genes show strong...
01:29Overview of Archaea
Archaea, named after the Archaean eon, represent a unique domain of life, distinct from bacteria and eukaryotes, with remarkable traits. Their cellular and molecular features, ecological adaptability, and industrial relevance highlight their importance in understanding life processes and leveraging biotechnology.Cellular and Molecular CharacteristicsA defining feature of archaea is their unique membrane composition. Archaeal membranes contain ether-linked isoprenoid lipids, which confer...
01:30Diversity of Archaea I
Archaea, a domain of single-celled microorganisms, are classified into five major phyla based on genetic and biochemical characteristics: Euryarchaeota, Crenarchaeota, Thaumarchaeota, Korarchaeota, and Nanoarchaeota. Among these, the phylum Euryarchaeota is notable for its remarkable diversity in morphology, metabolism, and ecological adaptations.Morphological and Metabolic DiversityMembers of Euryarchaeota exhibit a variety of cellular shapes, including rods and cocci. Their metabolic pathways...
01:27Diversity of Archaea III
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 environments.Morphological...
01:29Diversity of Archaea IV
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 thermal...