Standard assays do not predict the efficiency of commercial cellulase preparations towards plant materials

M.A. Kabel, M.J.E.C. van der Maarel, G. Klip, A.G.J. Voragen, H.A. Schols

Research output: Contribution to journalArticleAcademicpeer-review

85 Citations (Scopus)

Abstract

Commercial cellulase preparations are potentially effective for processing biomass feedstocks in order to obtain bioethanol. In plant cell walls, cellulose fibrils occur in close association with xylans (monocotyls) or xyloglucans (dicotyls). The enzymatic conversion of cellulose/xylans is a complex process involving the concerted action of exolendocellulases and cellobiases yielding glucose and xylanases yielding xylooligomers and xylose. An overview of commonly measured cellulase-, cellobiase-, and xylanase-activity, using respectively filter paper, cellobiose, and AZCL-dyed xylan as a substrate of 14 commercially available enzyme preparations from several suppliers is presented. In addition to these standardized tests, the enzyme-efficiency of degrading native substrates was studied. Grass and wheat bran were fractionated into a water unsoluble fraction (WUS), which was free of oligosaccharides and starch. Additionally, cellulose- and xylan-rich fractions were prepared by alkaline extraction of the WUS and were enzymatically digested. Hereby, the capability of cellulose and xylan conversion of the commercial enzyme preparations tested was measured. The results obtained showed that there was a large difference in the performance of the fourteen enzyme samples. Comparing all results, it was concluded that the choice of an enzyme preparation is more dependent on the characteristics of the substrate rather than on standard enzyme-activities measured
Original languageEnglish
Pages (from-to)56-63
JournalBiotechnology and Bioengineering
Volume93
Issue number1
DOIs
Publication statusPublished - 2006

Keywords

  • wheat bran
  • cell-wall
  • trichoderma-viride
  • selective extraction
  • ethanol
  • purification
  • degradation
  • endoglucanases
  • fractionation
  • components

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