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Functional stabilization of cellulase by covalent modification with chitosan
Author(s) -
Darias Rodolfo,
Villalonga Reynaldo
Publication year - 2001
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.386
Subject(s) - cellulase , thermostability , chitosan , trichoderma viride , thermal stability , chemistry , periodate , covalent bond , conjugate , chemical modification , enzyme , polymer , immobilized enzyme , polymer chemistry , nuclear chemistry , organic chemistry , food science , mathematical analysis , mathematics
Chitosan was linked to cellulase (EC 3.2.1.4) from Trichoderma viride by covalent conjugation to periodate‐activated carbohydrate moieties of the enzyme. The modified enzyme contained about 1.5 mol of polymer per mol of protein. The specific activity of the conjugate prepared was 39.8% of the native cellulase. The optimum pH and temperature for cellulase remained unaltered after modification. The thermostability was increased by 8.9 °C for the cellulase–chitosan complex. Thermal inactivation at different temperatures ranging from 65 °C to 80 °C was markedly increased for the polymer‐modified enzyme. The stability within the pH range 1.0–3.2 was also improved for the modified enzyme. © 2001 Society of Chemical Industry