title: Enzymatic deinking of secondary fibers: cellulases/hemicellulases versus laccase-mediator system.
abstract: The use of enzymes has been suggested as an environmentally friendly alternative to complement conventional chemical deinking in the recycling of recovered paper. This study compares the use of cellulases/hemicellulases versus the laccase-mediator system for deinking printed fibers from newspapers and magazines. For this purpose, two commercial enzyme preparations with endoglucanase and endoxylanase activities (Viscozyme Wheat from Aspergillus oryzae and Ultraflo L from Humicola insolens, Novozymes) and a commercial laccase (NS51002 from Trametes villosa, Novozymes), the latter in the presence of synthetic or natural (lignin-related) mediators, were evaluated. The enzymatic treatments were studied at the laboratory scale using a standard chemical deinking sequence consisting of a pulping stage; an alkaline stage using NaOH, sodium silicate and fatty acid soap; and a bleaching stage using hydrogen peroxide. The handsheets were then prepared and their brightness, residual ink concentration, and strength properties were measured. Among the different enzymatic treatments assayed, both carbohydrate hydrolases were found to deink the secondary fibers more efficiently. Brightness increased up to 3-4% ISO on newspaper fibers, being Ultraflo 20% more efficient in the ink removal. Up to 2.5% ISO brightness increase was obtained when magazine fibers were used, being Viscozyme 9% more efficient in the ink removal. Regarding the laccase-mediator system, alone or in combination with carbohydrate hydrolases, it was ineffective in deinking both newspaper and magazine fibers, resulting in pulps with worse brightness and residual ink concentration values. However, pulp deinking by the laccase-mediator system was displayed when secondary fibers from printed cardboard were used, obtaining up to 3% ISO brightness increase and lower residual ink concentrations.
authors.affiliation: Centro de Investigaciones Biológicas, Environmental Biology Department, CSIC, Ramiro de Maeztu 9, 28040, Madrid, Spain. david.ibarra@ciemat.es
authors.forename: David
authors.initials: D
authors.lastname: Ibarra
authors.forename: M
authors.initials: M
authors.lastname: Concepción Monte
authors.forename: Angeles
authors.initials: A
authors.lastname: Blanco
authors.forename: Angel T
authors.initials: AT
authors.lastname: Martínez
authors.forename: María J
authors.initials: MJ
authors.lastname: Martínez
mesh_terms: D002480:Cellulase / Q000378:metabolism; D044602:Cellulases / Q000378:metabolism*; D043364:Endo-1,4-beta Xylanases / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D007281:Ink; D042845:Laccase / Q000378:metabolism*; D008031:Lignin / Q000378:metabolism; D010209:Paper; D059027:Recycling / Q000379:methods
chemical_list: D008031:Lignin; D042845:Laccase; D044602:Cellulases; D006026:Glycoside Hydrolases; C023305:hemicellulase; D002480:Cellulase; D043364:Endo-1,4-beta Xylanases