Improvement of bacterial  -glucanase thermostability by glycosylation

Olsen, Ole; Thomsen, Kristine Rømer

doi:10.1099/00221287-137-3-579

Cited by 60 publications

(25 citation statements)

References 21 publications

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“…One of the two enzymes was strongly kinetically stabilized by glycosylation at 70°C, and its optimum temperature for activity was higher. The thermostabilization level depended more on the location of the carbohydrate moiety on the protein than on the extent of glycosylation (267). While glycosylation is probably not a thermostabilization method commonly found in nature, the few examples cited above suggest that it could represent an alternative method for either enzyme thermostabilization or for solubilization.…”

Section: Posttranslational Modificationsmentioning

confidence: 99%

Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability

Vieille¹,

Zeikus

2001

Microbiol Mol Biol Rev

1,870

1,476

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Enzymes synthesized by hyperthermophiles (bacteria and archaea with optimal growth temperatures of >80°C), also called hyperthermophilic enzymes, are typically thermostable (i.e., resistant to irreversible inactivation at high temperatures) and are optimally active at high temperatures. These enzymes share the same catalytic mechanisms with their mesophilic counterparts. When cloned and expressed in mesophilic hosts, hyperthermophilic enzymes usually retain their thermal properties, indicating that these properties are genetically encoded. Sequence alignments, amino acid content comparisons, crystal structure comparisons, and mutagenesis experiments indicate that hyperthermophilic enzymes are, indeed, very similar to their mesophilic homologues. No single mechanism is responsible for the remarkable stability of hyperthermophilic enzymes. Increased thermostability must be found, instead, in a small number of highly specific alterations that often do not obey any obvious traffic rules. After briefly discussing the diversity of hyperthermophilic organisms, this review concentrates on the remarkable thermostability of their enzymes. The biochemical and molecular properties of hyperthermophilic enzymes are described. Mechanisms responsible for protein inactivation are reviewed. The molecular mechanisms involved in protein thermostabilization are discussed, including ion pairs, hydrogen bonds, hydrophobic interactions, disulfide bridges, packing, decrease of the entropy of unfolding, and intersubunit interactions. Finally, current uses and potential applications of thermophilic and hyperthermophilic enzymes as research reagents and as catalysts for industrial processes are described

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Section: Posttranslational Modificationsmentioning

confidence: 99%

Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability

Vieille¹,

Zeikus

2001

Microbiol Mol Biol Rev

1,870

1,476

View full text Add to dashboard Cite

show abstract

“…Glycosylation can also alter the heat stability of proteins which has been shown for two different β -1 → 3/4 glucanases from Bacillus species. Expression in Saccharomyces cerevisiae resulted in heavily glycosylated enzymes (carbohydrate content of about 45%) which were significantly more heat stable than their non-glycosylated counterparts expressed in Escherichia coli [18]. Such findings are of special in- terest for the industrial use of proteins.…”

Section: Protective and Stabilizing Functionsmentioning

confidence: 83%

Glycoproteins: Properties

Wittmann

2008

Glycoscience

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“…19 ) Olsen et at. 20) studied the relationship between enzyme stability and glycosylation for the two different Bacillus (1,3-1 ,4)-f3-g1ucanases. However, the f3-g1ucosidase of Candida molischiana 35M5N was found to have similar kinetic properties to the wild-type.…”

Section: On Sds-pagementioning

confidence: 99%

A Very Stableβ-Glucosidase from aCandida molischianaMutant Strain: Enzymatic Properties, Sequencing, and Homology with Other Yeastβ-Glucosidases

Janbon

Derancourt

Chemardin

et al. 1995

Bioscience, Biotechnology, and Biochemistry

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Improvement of bacterial -glucanase thermostability by glycosylation

Abstract: The relationship between enzyme stability and glycosylation was examined for two different Bacillus (1,%1,4)-@-glucanases following expression of the corresponding genes in Escherkhiu coli and in Succhuromyces cerenisiae.

Cited by 60 publications

References 21 publications

Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability

Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability

Glycoproteins: Properties

A Very Stableβ-Glucosidase from aCandida molischianaMutant Strain: Enzymatic Properties, Sequencing, and Homology with Other Yeastβ-Glucosidases

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