Glycoside hydrolases (GHs, EC3.2.1) are enzymes that hydrolyze the glycosidic bonds of various sugary compounds (including monosaccharides, oligosaccharides, polysaccharides, saponins, and glycoproteins) by internal or external cleavage to form monosaccharides, oligosaccharides or glycoconjugates. They exist in almost all microorganisms and play an important role in the hydrolysis and synthesis of sugars and glycoconjugates. As a typical high-temperature habitat (>45 °C), hot springs contain abundant and unique thermophilic microorganisms and thermophilic GHs, which have become one of the research hotspots. In general, enzymes with thermophilic characteristics are of special interest for industrial applications where harsh conditions such as high temperatures. Thermophilic GHs such as cellulases, xylanases, amylases, chitinases, and other glucosidases, are widely used in food, bioenergy, feed, pharmaceutical, textile, and papermaking industries.
Due to the limitations of the current pure culture technology in the laboratory, more than 99% of prokaryotic microorganisms cannot be cultured, which limits us to explore thermophilic GHs. Many functions of GHs obtained by genomic or metagenomic technologies are only predicted based on bioinformatics data analysis and are not experimentally verified. Moreover, the high-temperature adaptation mechanism of thermophilic GHs from hot spring microorganisms has not been fully studied. Therefore, the research on thermophilic GHs from hot spring microorganisms is of great significance for mining new thermophilic GHs function genes and exploring their mechanism of high-temperature adaptation.
As a high-temperature habitat in nature, hot springs inhabit a wealth of thermophilic microorganisms, including fungi, bacteria, and archaea. These microorganisms are important sources of thermophilic GHs. The study of thermophilic GHs' adaptation to high temperatures is crucial for understanding the evolutionary mechanism of hot spring microorganisms. Therefore, the scope of the Research Topic is as follows:
(1) Identification of new thermophilic glycoside hydrolases (GHs) from hot spring microorganisms.
(2) New technologies and methods for mining thermophilic enzymes from hot springs, such as cellulases, xylanases, amylases, chitinases, and other glucosidases, etc.
(3) The changes in microbial community and the regulation mechanism of functional gene expression during the degradation of cellulose, hemicellulose, starch, chitin, and other polysaccharides as carbon sources by thermophilic microorganisms in hot spring.
(4) Reveal the high-temperature adaptation mechanism of thermophilic GHs from hot spring microorganisms at the evolutionary and molecular level.
Glycoside hydrolases (GHs, EC3.2.1) are enzymes that hydrolyze the glycosidic bonds of various sugary compounds (including monosaccharides, oligosaccharides, polysaccharides, saponins, and glycoproteins) by internal or external cleavage to form monosaccharides, oligosaccharides or glycoconjugates. They exist in almost all microorganisms and play an important role in the hydrolysis and synthesis of sugars and glycoconjugates. As a typical high-temperature habitat (>45 °C), hot springs contain abundant and unique thermophilic microorganisms and thermophilic GHs, which have become one of the research hotspots. In general, enzymes with thermophilic characteristics are of special interest for industrial applications where harsh conditions such as high temperatures. Thermophilic GHs such as cellulases, xylanases, amylases, chitinases, and other glucosidases, are widely used in food, bioenergy, feed, pharmaceutical, textile, and papermaking industries.
Due to the limitations of the current pure culture technology in the laboratory, more than 99% of prokaryotic microorganisms cannot be cultured, which limits us to explore thermophilic GHs. Many functions of GHs obtained by genomic or metagenomic technologies are only predicted based on bioinformatics data analysis and are not experimentally verified. Moreover, the high-temperature adaptation mechanism of thermophilic GHs from hot spring microorganisms has not been fully studied. Therefore, the research on thermophilic GHs from hot spring microorganisms is of great significance for mining new thermophilic GHs function genes and exploring their mechanism of high-temperature adaptation.
As a high-temperature habitat in nature, hot springs inhabit a wealth of thermophilic microorganisms, including fungi, bacteria, and archaea. These microorganisms are important sources of thermophilic GHs. The study of thermophilic GHs' adaptation to high temperatures is crucial for understanding the evolutionary mechanism of hot spring microorganisms. Therefore, the scope of the Research Topic is as follows:
(1) Identification of new thermophilic glycoside hydrolases (GHs) from hot spring microorganisms.
(2) New technologies and methods for mining thermophilic enzymes from hot springs, such as cellulases, xylanases, amylases, chitinases, and other glucosidases, etc.
(3) The changes in microbial community and the regulation mechanism of functional gene expression during the degradation of cellulose, hemicellulose, starch, chitin, and other polysaccharides as carbon sources by thermophilic microorganisms in hot spring.
(4) Reveal the high-temperature adaptation mechanism of thermophilic GHs from hot spring microorganisms at the evolutionary and molecular level.