Comparison of the adsorption properties of a single-chain antibody fragment fused to a fungal or bacterial cellulose-binding domain

T Reinikainen, K Takkinen, TT Teeri

Research output: Contribution to journalArticleScientificpeer-review

Abstract

Trichoderma reesei cellobiohydrolase I (CBHI) and Cellulomonas fimi cellulose-xylanase (Cex) both have distinct C-terminal cellulose-binding domains which belong to different CBD sequence families. Two fusion proteins comprising a single-chain antibody fragment (OxscFv) against 2-phenyloxazolone fused to the two CBDs (CBDCBHI or CBDCex) were constructed. The binding properties of the fusion proteins were studied on different cellulosic substrates. It was shown that the CBDCex binds the fusion protein to cellulose more effectively different cellulosic substrates. It was shown that the CBDCex binds the fusion protein to cellulose more effectively than the CBDCBHI; however, once immobilized, both fusion proteins could be eluted from cellulose only with denaturing agents or very low or high pH. Both fusion proteins retained equally well their ability to bind the hapten recognized by their antibody part. (C) 1997 by Elsevier Science Inc.

Original languageEnglish
Pages (from-to)143-149
Number of pages7
JournalEnzyme and Microbial Technology
Volume20
Issue number2
Publication statusPublished - 1 Feb 1997
MoE publication typeA1 Journal article-refereed

Keywords

  • cellulose
  • cellulose-binding domain
  • fusion protein
  • single-chain antibody
  • immobilization
  • REESEI CELLOBIOHYDROLASE-I
  • TRICHODERMA-REESEI
  • FUSION PROTEIN
  • TRYPTOPHAN RESIDUES
  • ESCHERICHIA-COLI
  • FIMI
  • EXOGLUCANASE
  • PURIFICATION
  • RESONANCE
  • FAMILIES

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