Thermophiles and thermophilic hydrolases

Ghosh, Shilpi; Lepcha, Khusboo; Basak, Arijita; Mahanty, Ayan Kumar

doi:10.1016/b978-0-12-818322-9.00016-2

Cited by 7 publications

(10 citation statements)

References 188 publications

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“…Cellulases have broad commercial applications because they convert lignocellulosic biomass into simple monosaccharides via enzymatic degradation, which can then be used to manufacture several valuable products in the industry ( Patel et al, 2019 ). Furthermore, cellulase can be used for many other applications, including waste management, pigment extraction, and bioactive molecules extraction from plant materials ( Ghosh et al, 2020 ). Thermostable cellulase is of great interest in the depolymerization of complex lignocellulose polymers.…”

Section: Cellulase and Xylanase Of Thermophilesmentioning

confidence: 99%

“…Many thermophilic bacteria have produced thermostable cellulolytic enzymes. These include Bacillus, Geobacillus, Caldibacillus, Acidothermus, Caldocellum, and Clostridium ( Ghosh et al, 2020 ). The Hyperthermophilic anaerobe Caldicellulosiruptor bescii, isolated from a Kamchatka hot spring, contained highly active cellulases.…”

Section: Cellulase and Xylanase Of Thermophilesmentioning

confidence: 99%

“…Thermophilic and hyperthermophilic bacteria such as Bacillus licheniformis ( Raj et al, 2018 ) Rhodothermus marinus ( Karlsson et al, 2004 ), Caldicoprobacter algeriensis ( Mhiri et al, 2020 ), Thermococcus zilligii , Sulfolobus solfataricus, and Pyrodictium abyssi have been extensively studied to produce highly thermostable xylanase. The majority of the xylanase produced from these thermophiles were identified to be members of families 10 and 11 of glycoside hydrolases (GH) ( Ghosh et al, 2020 ). Geobacillus sp.…”

Section: Cellulase and Xylanase Of Thermophilesmentioning

confidence: 99%

“…The sequence alignment of the amino acid, crystallographic, and mutagenesis studies indicate that several minor modifications contribute to the enhanced temperature stability of xylanases. There is hydrogen bonds and ion pairs, as well as disulfide network formation, specifically in the N- to C-terminals and α-helix, of thermophiles and thermophilic glycoside hydrolases, and aromatic residues which, as a result, lead to the formation of ‘sticky patches’ on the surface of the protein ( Ghosh et al, 2020 ).…”

Section: Strategies To Enhance Thermostability and Specific Activity Of Cellulase And Xylanase Of Thermophilesmentioning

confidence: 99%

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Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

Ajeje¹,

Hu²,

Song³

et al. 2021

Front. Bioeng. Biotechnol.

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The bioconversion of lignocellulose into monosaccharides is critical for ensuring the continual manufacturing of biofuels and value-added bioproducts. Enzymatic degradation, which has a high yield, low energy consumption, and enhanced selectivity, could be the most efficient and environmentally friendly technique for converting complex lignocellulose polymers to fermentable monosaccharides, and it is expected to make cellulases and xylanases the most demanded industrial enzymes. The widespread nature of thermophilic microorganisms allows them to proliferate on a variety of substrates and release substantial quantities of cellulases and xylanases, which makes them a great source of thermostable enzymes. The most significant breakthrough of lignocellulolytic enzymes lies in lignocellulose-deconstruction by enzymatic depolymerization of holocellulose into simple monosaccharides. However, commercially valuable thermostable cellulases and xylanases are challenging to produce in high enough quantities. Thus, the present review aims at giving an overview of the most recent thermostable cellulases and xylanases isolated from thermophilic and hyperthermophilic microbes. The emphasis is on recent advancements in manufacturing these enzymes in other mesophilic host and enhancement of catalytic activity as well as thermostability of thermophilic cellulases and xylanases, using genetic engineering as a promising and efficient technology for its economic production. Additionally, the biotechnological applications of thermostable cellulases and xylanases of thermophiles were also discussed.

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Section: Cellulase and Xylanase Of Thermophilesmentioning

confidence: 99%

Section: Cellulase and Xylanase Of Thermophilesmentioning

confidence: 99%

Section: Cellulase and Xylanase Of Thermophilesmentioning

confidence: 99%

Section: Strategies To Enhance Thermostability and Specific Activity Of Cellulase And Xylanase Of Thermophilesmentioning

confidence: 99%

See 2 more Smart Citations

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

Ajeje¹,

Hu²,

Song³

et al. 2021

Front. Bioeng. Biotechnol.

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“…The metabolic strategies of thermophiles are highly diverse. For a discussion, the reader is referred to [106].…”

Section: Nutrientsmentioning

confidence: 99%

¬Estimating Microbial Hydrogen Consumption in Hydrogen Storage in Porous Media as a Basis for Site Selection

Thaysen¹,

McMahon²,

Butler³

et al. 2020

Preprint

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Subsurface storage of hydrogen, e.g. in depleted gas or oil fields (DOGF), is suggested as a means to overcome imbalances between supply and demand in the renewable energy sector. However, hydrogen is an electron donor for subsurface microbial processes, which may have important implications for hydrogen recovery, gas injectivity and corrosion. Here, we review the controls on the three major hydrogen consuming processes in the subsurface, methanogenesis, homoacetogenesis, and sulfate reduction, as a basis to develop a hydrogen storage site selection tool. Testing our tool on 42 DOGF showed that seven of the fields may be considered sterile with respect to hydrogenconsuming microbiota due to either temperatures >122 °C or salinities >5 M NaCl. Only three fields can sustain all of the hydrogen consuming processes, due to either temperature, salinity or pressure constraints in the remaining fields. We calculated a potential microbial growth in the order of 1-17*10 7 cells ml-1 for these fields. The associated hydrogen consumption is negligible to small (<0.01-3.2 % of the stored hydrogen). Our results can help inform decisions about where hydrogen will be stored in the future.

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Exploration of computational approaches to predict the structural features and recent trends in α‐amylase production for industrial applications

Shad

Hussain

Usman

et al. 2023

Biotech & Bioengineering

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Amylases are biologically active enzymes that can hydrolyze starch to produce dextrin, glucose, maltose, and oligosaccharides. The amylases contribute approximately 30% to the global industrial enzyme market. The globally produced amylases are widely used in textile, biofuel, starch processing, food, bioremediation of environmental pollutants, pulp, and paper, clinical, and fermentation industries. The purpose of this review article is to summarize recent trends and aspects of α-amylases, classification, microbial production sources, biosynthesis and production methods, and its broad-spectrum applications for industrial purposes, which will depict the latest trends in α-amylases production. In the present article, we have comprehensively compared the biodiversity of α-amylases in different model organisms ranging from archaea to eukaryotes using in silico structural analysis tools. The detailed comparative analysis: regarding their structure, function, cofactor, signal peptide, and catalytic domain along with their catalytic residues of α-amylases in 16 model organisms were discussed in this paper. The comparative studies on alpha (α) amylases' secondary and tertiary structures, multiple sequence alignment, transmembrane helices, physiochemical properties, and their phylogenetic analysis in model organisms were briefly studied. This review has documented the recent trends and future perspectives of industrially important novel thermophilic α-amylases. In conclusion, this review sheds light on the current understanding and prospects of α-amylase research, highlighting its importance as a versatile enzyme with numerous applications and emphasizing the need for further exploration and innovation in this field.

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Thermophiles and thermophilic hydrolases

Cited by 7 publications

References 188 publications

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

¬Estimating Microbial Hydrogen Consumption in Hydrogen Storage in Porous Media as a Basis for Site Selection

Exploration of computational approaches to predict the structural features and recent trends in α‐amylase production for industrial applications

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