Mode of depolymerisation of hemicellulose by various mannanases and xylanases in relation to their ability to bleach softwood pulp

Endo-mannanases and endo-xylanases cleave different heteromannans and xylans yielding mainly dimers and trimers of the corresponding sugars as endproducts. However, in the early stages of hydrolysis, four purified mannanases and four xylanases from fungal and bacterial origin, examined in this study...

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Veröffentlicht in:Applied microbiology and biotechnology 1997-06, Vol.47 (6), p.658-662
Hauptverfasser: Gubitz, G.M, Haltrich, D, Latal, B, Steiner, W
Format: Artikel
Sprache:eng
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Zusammenfassung:Endo-mannanases and endo-xylanases cleave different heteromannans and xylans yielding mainly dimers and trimers of the corresponding sugars as endproducts. However, in the early stages of hydrolysis, four purified mannanases and four xylanases from fungal and bacterial origin, examined in this study, showed a different pattern of released oligomers (determined up to the pentamers). Furthermore, some of these enzymes showed a preference for cleaving the polysaccharides in the middle of the chain while others acted more at the end. When the increase in the specific fluidity of mannan and xylan solutions per reducing sugar released (Kv) was measured against the bleaching effect of the enzymes on softwood kraft pulp, a correlation was found. A xylanase from Penicillium simplicissimum (Kv = 0.15 l mPa-1 s-1 g-1) and a mannanase from Sclerotium rolfsii (Kv = 0.121 mPa-1 s-1 g-1) applied in a O(QX)P bleaching sequence (O = oxygen delignification, X = treatment with hemicellulolytic enzymes, Q = chelation of metals, P = treatment with hydrogen peroxide in alkaline solution) gave a high brightness increase of 3.0% and 1.9% ISO respectively. A less significant brightness increase was obtained with enzymes showing lower Kv values, such as a xylanase from Schizophyllum commune (Kv = 0.051 l mPa-1 s-1 g-1, 0.2% ISO) and a bacterial mannanase (Kv = 0.061 l mPa-1 s-1 g-1, 0.5% ISO).
ISSN:0175-7598
1432-0614
DOI:10.1007/s002530050991