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

doi:10.1016/S0141-0229(96)00109-3

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 journal › Article › Scientific › peer-review

12 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 (CBD_CBHI or CBD_Cex) were constructed. The binding properties of the fusion proteins were studied on different cellulosic substrates. It was shown that the CBD_Cex binds the fusion protein to cellulose more effectively than the CBD_CBHI; 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 language	English
Pages (from-to)	143 - 149
Number of pages	7
Journal	Enzyme and Microbial Technology
Volume	20
Issue number	2
DOIs	https://doi.org/10.1016/S0141-0229(96)00109-3
Publication status	Published - 1997
MoE publication type	A1 Journal article-refereed

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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.",

author = "Tapani Reinikainen and Kristiina Takkinen and Tuula Teeri",

note = "Project code: B5SU00132",

year = "1997",

doi = "10.1016/S0141-0229(96)00109-3",

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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

N1 - Project code: B5SU00132

PY - 1997

Y1 - 1997

N2 - 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.

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.

U2 - 10.1016/S0141-0229(96)00109-3

DO - 10.1016/S0141-0229(96)00109-3

M3 - Article

SN - 0141-0229

VL - 20

SP - 143

EP - 149

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

IS - 2

ER -

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

Abstract

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