Adsorption of monocomponent enzymes in enzyme mixture analyzed quantitatively during hydrolysis of lignocellulose substrates

Anikó Varnai (Corresponding Author), Liisa Viikari, Kaisa Marjamaa, Matti Siika-aho

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

The adsorption of purified Trichoderma reesei cellulases (TrCel7A, TrCel6A and TrCel5A) and xylanase TrXyn11 and Aspergillus niger β-glucosidase AnCel3A was studied in enzyme mixture during hydrolysis of two pretreated lignocellulosic materials, steam pretreated and catalytically delignified spruce, along with microcrystalline cellulose (Avicel). The enzyme mixture was compiled to resemble the composition of commercial cellulase preparations. The hydrolysis was carried out at 35 °C to mimic the temperature of the simultaneous saccharification and fermentation (SSF). Enzyme adsorption was followed by analyzing the activity and the protein amount of the individual free enzymes in the hydrolysis supernatant. Most enzymes adsorbed quickly at early stages of the hydrolysis and remained bound throughout the hydrolysis, although the conversion reached was fairly high. Only with the catalytically oxidized spruce samples, the bound enzymes started to be released as the hydrolysis degree reached 80%. The results based on enzyme activities and protein assay were in good accordance.
Original languageEnglish
Pages (from-to)1220-1227
Number of pages8
JournalBioresource Technology
Volume102
Issue number2
DOIs
Publication statusPublished - 2010
MoE publication typeA1 Journal article-refereed

    Fingerprint

Keywords

  • Lignocellulose
  • Cellulases
  • Enzymatic hydrolysis
  • Enzyme adsorption
  • Purified enzymes

Cite this