An α-L-arabinofuranosidase from Penicillium purpurogenum: Production, purification and properties

Pablo De Ioannes, Alessandra Peirano, Jeannette Steiner, Jaime Eyzaguirre

Resultado de la investigación: Article

50 Citas (Scopus)

Resumen

Penicillium purpurogenum secretes arabinofuranosidase to the growth medium. Highest levels of enzyme (1.0 U ml-1) are obtained when L-arabitol is used as carbon source, while 0.85 and 0.7 U ml-1 are produced with sugar beet pulp and oat spelts xylan, respectively. By means of a zymogram, three bands with arabinofuranosidase activity have been detected in the supernatant of a culture grown in oat spelts xylan. One of the enzymes was purified to homogeneity from this supernatant using gel filtration (BioGel P-100), cation exchange chromatography (CM-Sephadex C-50), hydrophobic interaction chromatography (phenyl agarose) and a second BioGel P-100 column. The enzyme is a monomer of 58 kDa with a pI of 6.5. Optimum pH is 4.0 and optimal temperature 50°C. The arabinofuranosidase is highly specific for α-L-arabinofuranosides and liberates arabinose from arabinoxylan. The enzyme shows hyperbolic kinetics towards p-nitrophenyl-α-L-arabinofuranoside with a K(M) of 1.23 mM. A 36-residue N-terminal sequence is over 70% identical to that of fungal arabinofuranosidases belonging to family 54 of the glycosyl hydrolases. Based on the sequence similarity and other biochemical properties it is proposed that the purified enzyme from P. purpurogenum belongs to family 54. Copyright (C) 2000 Elsevier Science B.V.

Idioma originalEnglish
Páginas (desde-hasta)253-258
Número de páginas6
PublicaciónJournal of Biotechnology
Volumen76
N.º2-3
DOI
EstadoPublished - 21 ene 2000

Huella dactilar

Penicillium
Purification
Enzymes
Xylans
Chromatography
Sugar beets
Hydrolases
Enzyme kinetics
Arabinose
Beta vulgaris
Hydrophobic and Hydrophilic Interactions
Pulp
Gel Chromatography
Cations
Ion exchange
Carbon
Gels
Monomers
Positive ions
Kinetics

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

Citar esto

De Ioannes, Pablo ; Peirano, Alessandra ; Steiner, Jeannette ; Eyzaguirre, Jaime. / An α-L-arabinofuranosidase from Penicillium purpurogenum : Production, purification and properties. En: Journal of Biotechnology. 2000 ; Vol. 76, N.º 2-3. pp. 253-258.
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abstract = "Penicillium purpurogenum secretes arabinofuranosidase to the growth medium. Highest levels of enzyme (1.0 U ml-1) are obtained when L-arabitol is used as carbon source, while 0.85 and 0.7 U ml-1 are produced with sugar beet pulp and oat spelts xylan, respectively. By means of a zymogram, three bands with arabinofuranosidase activity have been detected in the supernatant of a culture grown in oat spelts xylan. One of the enzymes was purified to homogeneity from this supernatant using gel filtration (BioGel P-100), cation exchange chromatography (CM-Sephadex C-50), hydrophobic interaction chromatography (phenyl agarose) and a second BioGel P-100 column. The enzyme is a monomer of 58 kDa with a pI of 6.5. Optimum pH is 4.0 and optimal temperature 50°C. The arabinofuranosidase is highly specific for α-L-arabinofuranosides and liberates arabinose from arabinoxylan. The enzyme shows hyperbolic kinetics towards p-nitrophenyl-α-L-arabinofuranoside with a K(M) of 1.23 mM. A 36-residue N-terminal sequence is over 70{\%} identical to that of fungal arabinofuranosidases belonging to family 54 of the glycosyl hydrolases. Based on the sequence similarity and other biochemical properties it is proposed that the purified enzyme from P. purpurogenum belongs to family 54. Copyright (C) 2000 Elsevier Science B.V.",
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An α-L-arabinofuranosidase from Penicillium purpurogenum : Production, purification and properties. / De Ioannes, Pablo; Peirano, Alessandra; Steiner, Jeannette; Eyzaguirre, Jaime.

En: Journal of Biotechnology, Vol. 76, N.º 2-3, 21.01.2000, p. 253-258.

Resultado de la investigación: Article

TY - JOUR

T1 - An α-L-arabinofuranosidase from Penicillium purpurogenum

T2 - Production, purification and properties

AU - De Ioannes, Pablo

AU - Peirano, Alessandra

AU - Steiner, Jeannette

AU - Eyzaguirre, Jaime

PY - 2000/1/21

Y1 - 2000/1/21

N2 - Penicillium purpurogenum secretes arabinofuranosidase to the growth medium. Highest levels of enzyme (1.0 U ml-1) are obtained when L-arabitol is used as carbon source, while 0.85 and 0.7 U ml-1 are produced with sugar beet pulp and oat spelts xylan, respectively. By means of a zymogram, three bands with arabinofuranosidase activity have been detected in the supernatant of a culture grown in oat spelts xylan. One of the enzymes was purified to homogeneity from this supernatant using gel filtration (BioGel P-100), cation exchange chromatography (CM-Sephadex C-50), hydrophobic interaction chromatography (phenyl agarose) and a second BioGel P-100 column. The enzyme is a monomer of 58 kDa with a pI of 6.5. Optimum pH is 4.0 and optimal temperature 50°C. The arabinofuranosidase is highly specific for α-L-arabinofuranosides and liberates arabinose from arabinoxylan. The enzyme shows hyperbolic kinetics towards p-nitrophenyl-α-L-arabinofuranoside with a K(M) of 1.23 mM. A 36-residue N-terminal sequence is over 70% identical to that of fungal arabinofuranosidases belonging to family 54 of the glycosyl hydrolases. Based on the sequence similarity and other biochemical properties it is proposed that the purified enzyme from P. purpurogenum belongs to family 54. Copyright (C) 2000 Elsevier Science B.V.

AB - Penicillium purpurogenum secretes arabinofuranosidase to the growth medium. Highest levels of enzyme (1.0 U ml-1) are obtained when L-arabitol is used as carbon source, while 0.85 and 0.7 U ml-1 are produced with sugar beet pulp and oat spelts xylan, respectively. By means of a zymogram, three bands with arabinofuranosidase activity have been detected in the supernatant of a culture grown in oat spelts xylan. One of the enzymes was purified to homogeneity from this supernatant using gel filtration (BioGel P-100), cation exchange chromatography (CM-Sephadex C-50), hydrophobic interaction chromatography (phenyl agarose) and a second BioGel P-100 column. The enzyme is a monomer of 58 kDa with a pI of 6.5. Optimum pH is 4.0 and optimal temperature 50°C. The arabinofuranosidase is highly specific for α-L-arabinofuranosides and liberates arabinose from arabinoxylan. The enzyme shows hyperbolic kinetics towards p-nitrophenyl-α-L-arabinofuranoside with a K(M) of 1.23 mM. A 36-residue N-terminal sequence is over 70% identical to that of fungal arabinofuranosidases belonging to family 54 of the glycosyl hydrolases. Based on the sequence similarity and other biochemical properties it is proposed that the purified enzyme from P. purpurogenum belongs to family 54. Copyright (C) 2000 Elsevier Science B.V.

KW - Arabinofuranosidase

KW - Enzyme purification

KW - Glycosyl hydrolase family 54

KW - Penicillium purpurogenum

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U2 - 10.1016/S0168-1656(99)00190-X

DO - 10.1016/S0168-1656(99)00190-X

M3 - Article

C2 - 10656340

AN - SCOPUS:0033991365

VL - 76

SP - 253

EP - 258

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

IS - 2-3

ER -