Purification and properties of an extracellular acidophilic endo-1,4-β-xylanase, naturally deleted in the "thumb", from Penicillium occitanis Pol6

Process Biochemistry

Volumn 46, Issue 6, 2011, Pages 1299-1306

  Driss, Dorra ^a   Bhiri, Fatma ^a   Elleuch, Lobna ^a   Bouly, Nathalie ^b,c   Stals, Ingeborg ^b,c   Miled, Nabil ^a   Blibech, Monia ^a   Ghorbel, Raoudha ^a   Chaabouni, Semia Ellouz ^a  

^a UNIVERSITY OF SFAX   (Tunisia)

^b UNIVERSITY COLLEGE GHENT   (Belgium)

^c GHENT UNIVERSITY   (Belgium)

Author keywords

DNA sequence; Endo 1,4 xylanase; Homology modeling; Penicillium occitanis Pol6; Purification

Indexed keywords

APPARENT K; CARBOHYDRATE CONTENT; CDNA ENCODING; CULTURE FILTRATE; ENDOXYLANASE; EXTRACELLULAR; FILAMENTOUS FUNGI; GENOMIC DNA; HOMOLOGY MODELING; MATURE PROTEINS; OPEN READING FRAME; PENICILLIUM OCCITANIS POL6; PURIFIED ENZYME; SDS-PAGE; SINGLE BAND; SPECIFIC ACTIVITY; XYLANASE ACTIVITY; XYLANASE INHIBITOR; XYLANASES; XYLOBIOSES; XYLOOLIGOSACCHARIDES;

AMINO ACIDS; CARBOHYDRATES; CLONING; DNA; DNA SEQUENCES; ENCODING (SYMBOLS); ENZYMES; NUCLEIC ACIDS; PURIFICATION;

ENZYME ACTIVITY;

FUNGI; PENICILLIUM; PENICILLIUM OCCITANIS; TRITICUM AESTIVUM SUBSP. SPELTA;

EID: 79955579577     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2011.02.022     Document Type: Article

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