Xylan-degrading enzymes from Aspergillus terreus: Physicochemical features and functional studies on hydrolysis of cellulose pulp

• Xylanases acted only on the hemicellulosic portion of cellulose pulps. • Affinity of phenolic compounds was higher for XylT1 as evidenced by K b values. • Increasing concentrations of quenchers caused a decrease in fluorescence intensity. • High concentrations of p-coumaric acid did not reduce flu...
Ausführliche Beschreibung

Gespeichert in:
Autor*in:

Moreira, Leonora Rios de Souza [verfasserIn]

Álvares, Alice da Cunha Morales

Jr, Francides Gomes da Silva

Freitas, Sonia Maria de

Filho, Edivaldo Ximenes Ferreira

Format:

E-Artikel

Sprache:

Englisch

Erschienen:

2015

Schlagwörter:

Potassium iodide (PubChem CID: 4875)

Orcinol (PubChem CID: 10436)

Sodium acetate (PubChem CID: 517045)

Sodium hydroxide (PubChem CID: 14798)

p-Coumaric acid (PubChem CID: 637542)

Acrylamide (PubChem CID: 6579)

Cesium chloride (PubChem CID: 24293)

3,5-Dinitrosalicylic acid (PubChem CID:11873)

Xylose (PubChem CID: 644160)

Vanillin (PubChem CID: 1183)

Umfang:

9

Übergeordnetes Werk:

Enthalten in: Residue co-evolution helps predict interaction sites in α-helical membrane proteins - Zeng, Bo ELSEVIER, 2019, an international journal devoted to scientific and technological aspects of industrially important polysaccharides, Amsterdam [u.a.]

Übergeordnetes Werk:

volume:134 ; year:2015 ; day:10 ; month:12 ; pages:700-708 ; extent:9

Links:

Volltext

DOI / URN:

10.1016/j.carbpol.2015.08.040

Katalog-ID:

ELV012763012

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