Erratum to: “Gene cloning, nucleotide sequence and biochemical properties of a cytoplasmic cyclomaltodextrinase (neopullulanase) from Alicyclobacillus acidocaldarius, reclassification of a group of enzymes” [FEMS Microbiol. Lett. 183 (2000) 55–61]

Matzke, Jutta; Herrmann, Anja; Schneider, Erwin; Bakker, Evert P.

doi:10.1016/s0378-1097(00)00188-9

Cited by 1 publication

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“…The genomes of thermophilic methanogenic archaea and hyperthermophilic bacteria are not much larger (1.6±1.8 megabases). These organisms, which all grow at higher temperatures than P. torridus, have to cope with a temperature dependent increased error rate in their nucleic acids due to cytosine deamination [31], which, amongst other factors, may have led to selective pressure favoring small genomes [30].…”

Section: Genomes From Thermoacidophilic Microorganismsmentioning

confidence: 99%

“…Four acid stable proteins have been purified and characterized. These include: a-amylase [35], cyclomaltodextrinase (neopullulanase) [31], maltose binding protein [36] and endoglucanase [37]. The a-amylase from this strain represents the first example of a heat and acid stable protein to have been studied in detail [38].…”

Section: Enzymes From Alicyclobacillus Acidocaldariusmentioning

confidence: 99%

“…Another gene from the thermoacidophilic bacterium A. acidocaldarius, encoding a cyclomaltodextrinase (neopullulanase), was cloned and its nucleotide sequence was determined [31]. The encoded CdaA protein lacked an N-terminal signal sequence and aligned well with a family of bacterial proteins described as maltogenic a-amylases, neopullulanases or cyclomaltodextrinases.…”

Section: Enzymes From Alicyclobacillus Acidocaldariusmentioning

confidence: 99%

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Thermoacidophilic Microorganisms and their Novel Biocatalysts

Bertoldo

Dock

Antranikian

2004

Engineering in Life Sciences

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Thermophilic acidophiles are microorganisms that are able to grow in pH and temperature ranges of 0.0–4.0 and 55–95 °C, respectively. Most of these microorganisms, which usually live in solfataric fields, belong to the archaea and include the genera Acidianus, Desulfurolobus, Metallosphaera, Stygiolobus, Sulfolobus, Sulfurisphaera, Sulfurococcus, Thermoplasma and Picrophilus. The sequencing of five complete genomes of thermoacidophilic organisms has allowed more detailed investigation regarding the evolution of organisms sharing extreme growth conditions of a unique niche, especially with respect to horizontal gene transfer. From such novel microorganisms, robust enzymes with potential biotechnological applications can be isolated. Enzymes that are optimally active at high temperature and extremely low pH are very rare and most of them are extracellular and involved in polymer degradation. Heat and acid stable α‐amylase, cyclomaltodextrinase (neopullulanase), maltose binding protein and endoglucanase have been purified and characterized from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius. Archaeal glycosyl hydrolases have been characterized from Picrophilus torridus, Picrophilus oshima, Thermoplasma acidophilum and Sulfolobus solfataricus. Biotransformation reactions can be performed even at pH close to zero and temperatures of 100 °C.

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Section: Genomes From Thermoacidophilic Microorganismsmentioning

confidence: 99%