Beta‐glucosidase from Penicillium purpurogenum: purification and properties.“

M. Hidalgo, J. Steiner, J. Eyzaguirre

Resultado de la investigación: Article

39 Citas (Scopus)

Resumen

beta‐Glucosidase was purified from the culture supernatant of Penicillium purpurogenum. The purified enzyme was homogeneous on both nondenaturing and sodium dodecyl sulfate (SDS)‐polyacrylamide gel electrophoresis. The enzyme is a monomeric glycoprotein with M(r) of 90,000 as determined by gel filtration on Bio‐Gel P‐300 and SDS‐polyacrylamide gels. Two enzyme forms were resolved by chromatofocusing and isoelectric focusing, and the pI values obtained with both methods were 4.2 (major form) and 6.0. The major form was characterised further. Enzyme activity was optimal at pH 3.5 and at 60 degrees C. The enzyme was stable in the pH range 2.5–9.5 for 24 h at 4 degrees C. Kinetic analysis gave Kms of 0.8 mM for cellobiose and 85 microM for p‐nitrophenyl‐beta‐D‐glucopyranoside. The enzyme hydrolyses a wide range of substrates including aryl‐beta‐glucosides, cellobiose, and amygdalin. Glucose inhibits competitively and glucono‐delta‐lactone is a mixed inhibitor of the enzyme. 1992 The Swiss Political Science Review

Idioma originalEnglish
Páginas (desde-hasta)185-191
Número de páginas7
PublicaciónBiotechnology and Applied Biochemistry
Volumen15
N.º2
DOI
EstadoPublished - 1 ene 1992

Huella dactilar

Penicillium
Purification
Enzymes
Cellobiose
Gels
Amygdalin
Enzyme activity
Enzyme Inhibitors
Glycoproteins
Electrophoresis
Sodium Dodecyl Sulfate
Isoelectric Focusing
Sodium dodecyl sulfate
Hydrolysis
Polyacrylates
Gel Chromatography
Glucose
Polyacrylamide Gel Electrophoresis
Kinetics
Substrates

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Molecular Medicine
  • Biomedical Engineering
  • Applied Microbiology and Biotechnology
  • Drug Discovery
  • Process Chemistry and Technology

Citar esto

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Beta‐glucosidase from Penicillium purpurogenum : purification and properties.“. / Hidalgo, M.; Steiner, J.; Eyzaguirre, J.

En: Biotechnology and Applied Biochemistry, Vol. 15, N.º 2, 01.01.1992, p. 185-191.

Resultado de la investigación: Article

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AU - Eyzaguirre, J.

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AB - beta‐Glucosidase was purified from the culture supernatant of Penicillium purpurogenum. The purified enzyme was homogeneous on both nondenaturing and sodium dodecyl sulfate (SDS)‐polyacrylamide gel electrophoresis. The enzyme is a monomeric glycoprotein with M(r) of 90,000 as determined by gel filtration on Bio‐Gel P‐300 and SDS‐polyacrylamide gels. Two enzyme forms were resolved by chromatofocusing and isoelectric focusing, and the pI values obtained with both methods were 4.2 (major form) and 6.0. The major form was characterised further. Enzyme activity was optimal at pH 3.5 and at 60 degrees C. The enzyme was stable in the pH range 2.5–9.5 for 24 h at 4 degrees C. Kinetic analysis gave Kms of 0.8 mM for cellobiose and 85 microM for p‐nitrophenyl‐beta‐D‐glucopyranoside. The enzyme hydrolyses a wide range of substrates including aryl‐beta‐glucosides, cellobiose, and amygdalin. Glucose inhibits competitively and glucono‐delta‐lactone is a mixed inhibitor of the enzyme. 1992 The Swiss Political Science Review

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