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Documentos Principais

T8778

Sigma-Aldrich

Trehalase from porcine kidney

buffered aqueous glycerol solution, ≥1.0 units/mg protein

Sinônimo(s):

α,α-Trehalose glucohydrolase

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About This Item

Número CAS:
Número da licença da enzima:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

Formulário

buffered aqueous glycerol solution

Nível de qualidade

atividade específica

≥1.0 units/mg protein

concentração

0.5-10.0 mg/mL protein (BCA)

temperatura de armazenamento

−20°C

Descrição geral

Trehalase is a glycosidase that occurs in many forms and is found in all tissues. It belongs to the glycoside hydrolase 37 (GH37) family of the carbohydrate-active enzyme (CAZy) classification.
Trehalose is the main haemolymph sugar in most insects and is potentially a prime target for an invading pathogenic fungus.

Aplicação

Trehalase has been used:
  • in a study to assess changes in carbohydrate metabolism in Plasmopara viticola-infected grapevine leaves
  • in a study to investigate growth arrest by trehalose-6-phosphate
  • to quantify the intracellular trehalose in Lactobacillus casei cells

Ações bioquímicas/fisiológicas

Trehalase catalyzes the hydrolysis of trehalose to produce two glucose units. It mediates flight metabolism, molting induced chitin production and tolerance towards cold temperature.

Definição da unidade

One unit will convert 1.0 μmole of trehalose to 2.0 μmoles of glucose per min at pH 5.7 at 37 °C (liberated glucose determined at pH 7.5).

forma física

Solution in 50% glycerol containing 1% Triton X-100 and 25 mM potassium phosphate, pH 6.5

Informações legais

Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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Growth arrest by trehalose-6-phosphate: an astonishing case of primary metabolite control over growth by way of the SnRK1 signaling pathway
Delatte, T., et al.
Annual review of plant physiology and plant molecular biology, 157, 160-174 (2011)
Wim Schepers et al.
The Journal of biological chemistry, 287(53), 44130-44142 (2012-11-17)
The readdition of an essential nutrient to starved, fermenting cells of the yeast Saccharomyces cerevisiae triggers rapid activation of the protein kinase A (PKA) pathway. Trehalase is activated 5-10-fold within minutes and has been used as a convenient reporter for
Choowong Auesukaree et al.
Journal of bioscience and bioengineering, 114(2), 144-149 (2012-05-15)
For industrial applications, fermentation of ethanol at high temperature offers advantages such as reduction in cooling costs, reduced risk of microbial contamination and higher efficiency of fermentation processes including saccharification and continuous ethanol stripping. Three thermotolerant Saccharomyces cerevisiae isolates (C3723
Dimitri A Skandalis et al.
Physiological and biochemical zoology : PBZ, 85(6), 657-670 (2012-10-27)
Although intraspecific variation in metabolic rate is associated with variation in body size, similarly sized individuals nonetheless vary greatly. At similar masses, hovering bumblebee workers (Bombus impatiens) can differ in metabolic rate up to twofold. We examined how such interindividual
Shari Dhaene et al.
Journal of enzyme inhibition and medicinal chemistry, 35(1), 1964-1989 (2020-11-10)
Although trehalose has recently gained interest because of its pharmaceutical potential, its clinical use is hampered due to its low bioavailability. Hence, hydrolysis-resistant trehalose analogues retaining biological activity could be of interest. In this study, 34 4- and 6-O-substituted trehalose

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