Literature DB >> 24420197

The role of fungal polysaccharidases in the hydrolysis of cell wall materials from sunflower and palm-kernel meals.

E M Düsterhöft1, A W Bonte, J C Venekamp, A G Voragen.   

Abstract

Main fractions from multi-component polysaccharidase preparations (Driselase, Gamanase and an experimental preparation of fungal origin), previously used for the enzymic treatment of cell wall materials from sunflower and palm-kernel meals, were sub-fractionated by different chromatographic techniques to evaluate the contribution of each of their constituent activities in cell wall degradation. Based on activity measurements, 5- to 10-fold purification was achieved for the major enzymes but residual side-activities were still detectable in most sub-fractions. Solubilization of non-starch polysaccharides from the cell wall materials by the resulting pectolytic, xylanolytic, cellulolytic and mannanolytic sub-fractions and by highly purified glucanases, arabinanases and xylanases was, when acting individually, very low (1% to 5%). With few exceptions, the solubilizing effect of the main fractions could only be slightly enhanced by supplementation with pectolytic, cellulolytic or mannanolytic sub-fractions or by highly purified enzymes. The extent of solubilization remained mostly lower than the sum of both individually obtained values. In the degradation of palm-kernel cell wall material, however, synergistic action of mannanases and glucanases was observed. The hydrolysis of pectic compounds in sunflower cell wall material was most effective when polygalacturonases, arabinanases and rhamnogalacturonan-degrading activities were applied together. The resistance of 4-O-methyl-glucuronoxylan, the major hemicellulosic polymer in the cell wall material from sunflower meal, to enzymic hydrolysis was not only caused by its location in the cell wall or interlinkage to other polymers but also by its primary structure. Neither purified endo-xylanase nor the crude parent preparation were able to achieve complete hydrolysis of this polysaccharide after extraction.

Entities:  

Year:  1993        PMID: 24420197     DOI: 10.1007/BF00386291

Source DB:  PubMed          Journal:  World J Microbiol Biotechnol        ISSN: 0959-3993            Impact factor:   3.312


  10 in total

1.  Assay of proteins in the presence of interfering materials.

Authors:  A Bensadoun; D Weinstein
Journal:  Anal Biochem       Date:  1976-01       Impact factor: 3.365

Review 2.  Digestion of non-starch polysaccharides by non-ruminant omnivores.

Authors:  J C Mathers
Journal:  Proc Nutr Soc       Date:  1991-08       Impact factor: 6.297

3.  Notes on sugar determination.

Authors:  M SMOGYI
Journal:  J Biol Chem       Date:  1952-03       Impact factor: 5.157

4.  Enzymic Studies of the Distribution Pattern of 4-O-Methylglucuronic Acid Residues in Glucuronoxylans from Sunflower Hulls.

Authors:  A Bazus; L Rigal; T Fontaine; B Fournet; M Gosselin; P Debeire
Journal:  Biosci Biotechnol Biochem       Date:  1992-01       Impact factor: 2.043

5.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

6.  Purification and properties of an exo-cellulase of Avicelase type from a wood-rotting fungus, Irpex lacteus (Polyporus tulipiferae).

Authors:  T Kanda; S Nakakubo; K Wakabayashi; K Nisizawa
Journal:  J Biochem       Date:  1978-11       Impact factor: 3.387

7.  Glycoprotein enzymes secreted by Aspergillus niger: purification and properties of alpha-glaactosidase.

Authors:  S Adya; A D Elbein
Journal:  J Bacteriol       Date:  1977-02       Impact factor: 3.490

8.  Purification and properties of a lower-molecular-weight endo-cellulase from Irpex lacteus (Polyporus tulipiferae).

Authors:  T Kanda; K Wakabayashi; K Nisizawa
Journal:  J Biochem       Date:  1980-06       Impact factor: 3.387

9.  Purification and properties of two endo-1,4-beta-xylanases from Irpex lacteus (Polyporus tulipiferae).

Authors:  T Kanda; Y Amano; K Nisizawa
Journal:  J Biochem       Date:  1985-12       Impact factor: 3.387

10.  The cellulase of Trichoderma viride. Purification, characterization and comparison of all detectable endoglucanases, exoglucanases and beta-glucosidases.

Authors:  G Beldman; M F Searle-Van Leeuwen; F M Rombouts; F G Voragen
Journal:  Eur J Biochem       Date:  1985-01-15
  10 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.