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

Tapani Reinikainen, Kristiina Takkinen, Tuula Teeri (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

10 Citations (Scopus)

Abstract

Trichoderma reesei cellobiohydrolase I (CBHI) and Cellulomonas fimi cellulase-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 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.

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

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Single-Chain Antibodies
Immunoglobulin Fragments
Antibodies
Cellulose
Adsorption
Fusion reactions
Proteins
Cellulomonas
Cellulose 1,4-beta-Cellobiosidase
Trichoderma
Cellulase
Haptens
Substrates

Cite this

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title = "Comparison of the adsorption properties of a single-chain antibody fragment fused to a fungal or bacterial cellulose-binding domain",
abstract = "Trichoderma reesei cellobiohydrolase I (CBHI) and Cellulomonas fimi cellulase-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 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.",
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Comparison of the adsorption properties of a single-chain antibody fragment fused to a fungal or bacterial cellulose-binding domain. / Reinikainen, Tapani; Takkinen, Kristiina; Teeri, Tuula (Corresponding Author).

In: Enzyme and Microbial Technology, Vol. 20, No. 2, 1997, p. 143 - 149.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Comparison of the adsorption properties of a single-chain antibody fragment fused to a fungal or bacterial cellulose-binding domain

AU - Reinikainen, Tapani

AU - Takkinen, Kristiina

AU - Teeri, Tuula

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PY - 1997

Y1 - 1997

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AB - Trichoderma reesei cellobiohydrolase I (CBHI) and Cellulomonas fimi cellulase-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 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.

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