Extremophiles as a source for novel enzymes

Burg, Bertus van den

doi:10.1016/s1369-5274(03)00060-2

Cited by 484 publications

(212 citation statements)

References 47 publications

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“…Alternatively, thiosulfate or sulfur can also be used as energy sources. Due to their thermostability, many of the enzymes found in the genus Aquifex and other thermophilic bacteria are of interest for industrial and biotechnological applications van den Burg, 2003).…”

Section: Introductionmentioning

confidence: 99%

Molecular signatures in protein sequences that are characteristics of the phylum Aquificae

Griffiths

2006

INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLO

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Section: Introductionmentioning

confidence: 99%

Molecular signatures in protein sequences that are characteristics of the phylum Aquificae

Griffiths

2006

INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLO

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“…The results showed that the thermodynamic parameters of the enzymes varied considerably among the different isolates, which suggests important variations in the thermo-properties of the proteases in this environment relative to bacterial original genus. In addition, enzymes produced by psychrophilics can offer biotechnological advantages to be used in different areas, such as food processing, laundry powder for cold-water washing, leather industry as well as in the treatment of effluents and bioremediation of polluted soils and waste waters in cold environment (Demain 1999, Van den Burg 2003. Moreover, the capacity of these psychrophilic microorganisms, including S. aquimarina and A. antarcticus, to grow and produce enzymes at low temperatures is beneficial as it fosters substantial energy saving in large scale enzyme production processes, since there is no need to heat up bioreactors (Margesin and Feller 2010).…”

Section: Discussionmentioning

confidence: 99%

Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil

Santos

Pires

Jesus

et al. 2015

An. Acad. Bras. Ciênc.

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Two psychrophilic bacterial samples were isolated from King George Island soil, in Antarctica. The phylogenetic analysis based on the 16S rRNA (rrs) gene led to the correlation with the closest related isolates as Sporosarcina aquimarina (99%) and Algoriphagus antarcticus (99%), with query coverage of 99% and 98%, respectively. The spent culture media from both isolates displayed proteolytic activities detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis containing gelatin as protein substrate. Under the employed conditions, S. aquimarina showed a 55 kDa protease with the best activity detected at pH 7.0 and at 27°C. A. antarcticus also showed a single extracellular protease, however its molecular mass was around 90kDa and its best activity was detected at pH 9.0 and at 37°C. The proteases from both isolates were inhibited by 1,10-phenanthroline and EDTA, two metalloprotease inhibitors. This is the first record of protease detection in both species, and our results may contribute to broaden the basic knowledge of proteases from the Antarctica environment and may help prospecting future biotechnological applications of these enzymes.

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Section: Hyperthermophilic Glucoside Hydrolasesmentioning

confidence: 99%

“…Potentially, extremozymes would enable us to expand the range of reaction conditions suitable for biocatalysis. This has proven to be the case and various applications in sugar chemistry, detergent production, lipid and oil chemistry, and food processing have been initiated or are being explored [20,21].Thermophilic microorganisms have attracted most attention, among which the most studies are toward the extremophile. Thermophiles can be generally classified into moderate thermophiles (growth optimum temp 50-60 °C), extreme thermophiles (growth optimum temp 60-80 °C) and hyperthermophiles (growth optimum temp 80-110 °C).…”

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Extremophilic Carbohydrate Active Enzymes (CAZymes)

Lee¹,

Park²,

Park³

2017

JNHFE

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Carbohydrate active enzymes (CAZymes) are a large class of enzymes, which build and breakdown the complex carbohydrates of the cell. On the basis of their amino acid sequences they are classified in families that show conserved catalytic mechanism, structure, and active site residues, but may conflict each other in substrate specificity. The CAZymes provides a continuously updated list of the glycoside hydrolase families, GHs. This group of enzymes is classified based on functional similarity, but today they are classified into 108 GHs on the basis of amino acid sequence similarity. Despite their similarities to enzymes with known functions, their primary functions are still unclear. Based on these criteria, β-galactosidase activities are now divided into four different families: GH1, GH2, GH35 and GH42, among which the better studied GH2 includes β-galactosidase from Escherichia coli, Aspergillus, Bacillus megatherium, and Sulfolobus solfataricus, while those from thermophilic, psychrophilic and halophilic organisms belong to GH42. Lactase is often confused as an alternate name for β-galactosidase, but it is actually simply a subclass (small subunit) of β-galactosidase.(β-D-galactoside galactohydrolase, EC 3.2.1.23) that catalyses hydrolysis of the galactosyl moiety from non-reducing termini of oligosaccharides or from glycosides. Most genes encoding GH42 enzymes are from prokaryotes that are unable to grow on lactose as a sole carbon source and at least two GH42 β-galactosidase do not cleave lactose in vitro. The determination of growth on lactose can be complicated by the multiple β-galactosidases because not all of the β-galactosidase is acting as lactases in vitro. Β-Galactosidase hydrolyses the β-1, 4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-β-dgalactopyranoside (ONPG), p-nitrophenyl-β-d-galactopyranoside (PNPG) and 6-bromo-2-naphthyl-galactopyranoside (BNG). This enzyme has been purified and characterized from various sources, including plants, animals, and many microorganisms. In humans, lactase is present predominantly along the brush border membrane of the differentiated enterocytes lining the villi of the small intestine. Lactase is essential for digestive hydrolysis of lactose in milk. Deficiency of the enzyme causes lactose intolerance. Several 3D structures are available for the GH1 and GH2 β-galactosidase for which the catalytic residues have experimentally been determined, while three 3D structures of β-galactosidase from E. coli, Penicillium sp and Thermus thermophilus A4 are available for both the GH35 and GH42 families. Glycoside hydrolasesGlycoside hydrolases are enzymes that catalyze the hydrolysis of the glycosidic linkage of glycosides, leading to the formation of a sugar hemiacetal or hemiketal and the corresponding free aglycon. Glycoside hydrolases are also referred to as glycosidases, and sometimes also as glycosyl hydrolases. Glycoside hydrolases can catalyze the hydrolysis of O-, N-and S-linked glycosides ( Figure 1). Endo/Exo:Exo / ...

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Extremophiles as a source for novel enzymes

Cited by 484 publications

References 47 publications

Molecular signatures in protein sequences that are characteristics of the phylum Aquificae

Molecular signatures in protein sequences that are characteristics of the phylum Aquificae

Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil

Extremophilic Carbohydrate Active Enzymes (CAZymes)

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