Acidophiles are ecologically and economically important group of microorganisms, which thrive in acidic natural (solfataric fields, sulfuric pools) as well as artificial man-made (areas associated with human activities such as mining of coal and metal ores) environments. They possess networked cellular adaptations to regulate pH inside the cell. Several extracellular enzymes from acidophiles are known to be functional at much lower pH than the cytoplasmic pH. Enzymes like amylases, proteases, ligases, cellulases, xylanases, α-glucosidases, endoglucanases, and esterases stable at low pH are known from various acidophilic microbes. The possibility of improving them by genetic engineering and directed evolution will further boost their industrial applications. Besides biocatalysts, other biomolecules such as plasmids, rusticynin, and maltose-binding protein have also been reported from acidophiles. Some strategies for circumventing the problems encountered in expressing genes encoding proteins from extreme acidophiles have been suggested. The investigations on the analysis of crystal structures of some acidophilic proteins have thrown light on their acid stability. Attempts are being made to use thermoacidophilic microbes for biofuel production from lignocellulosic biomass. The enzymes from acidophiles are mainly used in polymer degradation.
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http://dx.doi.org/10.1007/s00792-011-0402-3 | DOI Listing |
Food Res Int
January 2025
State Key Laboratory of Marine Food Processing and Safety Control, Dalian Polytechnic University, Dalian 116034, Liaoning, China. Electronic address:
The acidophilic and heat-resistant characteristics of Alicyclobacillus acidoterrestris (A. acidoterrestris) pose significant challenges to fruit juice production. Traditional thermal removal methods are often ineffective against this resilient bacterium.
View Article and Find Full Text PDFFood Chem
February 2025
College of Food Science and Engineering, Northwest A&F University, 22 Xinong Road, Yangling 712100, Shaanxi, China. Electronic address:
The acidophilic and heat-resistant traits of Alicyclobacillus acidoterrestris (A. acidoterrestris) present a formidable challenge to fruit juices production safety. To address the limitations of conventional thermal sterilization, a novel bacterial capture device MPDEL has been developed.
View Article and Find Full Text PDFExtremophiles
November 2024
The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, People's Republic of China.
The cell membrane remodeling mediated by cyclopropane fatty acid synthase (CfaS) plays a crucial role in microbial physiological processes resisting various environmental stressors, including acid. Herein, we found a relatively high proportion (24.8%-28.
View Article and Find Full Text PDFFEMS Microbiol Ecol
November 2024
School of Science, Edith Cowan University, Joondalup, WA 6027, Australia.
In-depth comparative genomic analysis was conducted to predict carbon, nitrogen, and phosphate assimilation pathways in the halotolerant, acidophilic genus Acidihalobacter. The study primarily aimed to understand how the metabolic capabilities of each species can determine their roles and effects on the microbial ecology of their unique saline and acidic environments, as well as in their potential application to saline water bioleaching systems. All four genomes encoded the genes for the complete tricarboxylic acid cycle, including 2-oxoglutarate dehydrogenase, a key enzyme absent in obligate chemolithotrophic acidophiles.
View Article and Find Full Text PDFFEMS Microbiol Ecol
August 2024
Centre for Environmental Biotechnology, School of Environmental and Natural Sciences, Bangor University, Bangor, LL57 2UW, United Kingdom.
Family GH1 glycosyl hydrolases are ubiquitous in prokaryotes and eukaryotes and are utilized in numerous industrial applications, including bioconversion of lignocelluloses. In this study, hyperacidophilic archaeon Cuniculiplasma divulgatum (S5T=JCM 30642T) was explored as a source of novel carbohydrate-active enzymes. The genome of C.
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