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Literature summary extracted from

  • Diaz, A.; Sieiro, C.; Villa, T.G.
    Production and partial characterization of a beta-amylase by Xanthophyllomyces dendrorhous (2003), Lett. Appl. Microbiol., 36, 203-207.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.2 additional information the synthesis of beta-amylase is induced by starch and maltose Phaffia rhodozyma

Application

EC Number Application Comment Organism
3.2.1.2 nutrition beta-amylase may have certain industrial applications, e.g. in the beer industry or in the production of maltose syrup, beta-amylase could be a by-product, in addition to carotenoid pigments, in the fermentation downstream Phaffia rhodozyma

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.2 HgCl2 10 mM, 100% inhibition Phaffia rhodozyma
3.2.1.2 additional information the synthesis of beta-amylase is repressed by glucose, fructose or sucrose as carbon source, not inhibited by EDTA Phaffia rhodozyma
3.2.1.2 N-bromosuccinimide 1 mM, 84% inhibition Phaffia rhodozyma
3.2.1.2 N-ethylmaleimide 10 mM, 73% inhibition Phaffia rhodozyma
3.2.1.2 p-hydroxymercuribenzoate 0.5 mM, 96% inhibition Phaffia rhodozyma
3.2.1.2 p-methylsulfonylfluoride 3 mM, 100% inhibition Phaffia rhodozyma
3.2.1.2 Phenylglyoxal 3 mM, 27% inhibition Phaffia rhodozyma

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.2 additional information
-
additional information
-
Phaffia rhodozyma

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.2 extracellular
-
Phaffia rhodozyma
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.2 240000
-
gel filtration Phaffia rhodozyma

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Phaffia rhodozyma
-
the perfect state of Phaffia rhodozyma
-
3.2.1.2 Phaffia rhodozyma CECT 1690
-
the perfect state of Phaffia rhodozyma
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.2 partial, 14.67fold Phaffia rhodozyma

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.2 (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion, the term beta relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed Phaffia rhodozyma

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.2 0.0685
-
pH 5.5, 50°C Phaffia rhodozyma

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 maltopentose + H2O 40% of the activity with starch, exo-acting enzyme, no production of glucose Phaffia rhodozyma ?
-
?
3.2.1.2 maltopentose + H2O 40% of the activity with starch, exo-acting enzyme, no production of glucose Phaffia rhodozyma CECT 1690 ?
-
?
3.2.1.2 maltotetraose + H2O 37% of the activity with starch, exo-acting enzyme, no production of glucose Phaffia rhodozyma ?
-
?
3.2.1.2 maltotetraose + H2O 37% of the activity with starch, exo-acting enzyme, no production of glucose Phaffia rhodozyma CECT 1690 ?
-
?
3.2.1.2 additional information cysteine, tryptophan and serine are essential amino acids for catalysis, not: maltotriose Phaffia rhodozyma ?
-
?
3.2.1.2 additional information cysteine, tryptophan and serine are essential amino acids for catalysis, not: maltotriose Phaffia rhodozyma CECT 1690 ?
-
?
3.2.1.2 starch + H2O highest activity, exo-acting enzyme, no production of glucose Phaffia rhodozyma ?
-
?
3.2.1.2 starch + H2O highest activity, exo-acting enzyme, no production of glucose Phaffia rhodozyma CECT 1690 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.2 beta-amylase
-
Phaffia rhodozyma

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 50
-
-
Phaffia rhodozyma

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.2 20 60 active in the range Phaffia rhodozyma

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.2 60
-
30 min: 65% loss of activity, 60 min: 75% loss of activity, 90 min: 100% loss of activity Phaffia rhodozyma

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 5.5
-
-
Phaffia rhodozyma

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.2 4 6.5 active in the range Phaffia rhodozyma

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.2 7.5
-
30 min: 50% loss of activity, 60 min: 75% loss of activity, 120 min: 100% loss of activity Phaffia rhodozyma

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.2 Phaffia rhodozyma isoelectric focusing 4.7 4.6