Molecular engineering of a thermostable carbohydrate-binding module
Cicortas Gunnarsson, Lavinia LU ; Nordberg Karlsson, Eva LU
; Andersson, Mats
; Holst, Olle
LU
and Ohlin, Mats
LU
(2006)
Sixth Carbohydrate Bioengineering Meeting
24(1-2).
p.31-37
- Abstract
- Structure-function studies are frequently practiced on the very diverse group of natural carbohydrate-binding modules in order to understand the target recognition of these proteins. We have taken a step further in the study of carbohydrate-binding modules and created variants with novel binding properties by molecular engineering of one such molecule of known 3D-structure. A combinatorial library was created from the sequence encoding a thermostable carbohydrate-binding module, CBM4-2 from a Rhodothermus marinus xylanase, and phage-display technology was successfully used for selection of variants with specificity towards different carbohydrate polymers (birchwood xylan, Avicel (TM), ivory nut mannan and recently also xyloglucan), as well... (More)
- Structure-function studies are frequently practiced on the very diverse group of natural carbohydrate-binding modules in order to understand the target recognition of these proteins. We have taken a step further in the study of carbohydrate-binding modules and created variants with novel binding properties by molecular engineering of one such molecule of known 3D-structure. A combinatorial library was created from the sequence encoding a thermostable carbohydrate-binding module, CBM4-2 from a Rhodothermus marinus xylanase, and phage-display technology was successfully used for selection of variants with specificity towards different carbohydrate polymers (birchwood xylan, Avicel (TM), ivory nut mannan and recently also xyloglucan), as well as towards a glycoprotein (human IgG4). Our work not only generated a number of binders with properties that would suite a range of biotechnological applications, but analysis of selected binders also helped us to identify residues important for their specificities. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/401453
- author
- Cicortas Gunnarsson, Lavinia
LU
; Nordberg Karlsson, Eva
LU
; Andersson, Mats
; Holst, Olle
LU
and Ohlin, Mats
LU
- organization
- publishing date
- 2006
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- subject
- keywords
- carbohydrate-binding module, binding specificity, combinatorial, library, molecular engineering, phage-display, protein scaffold
- host publication
- Biocatalysis and Biotransformation
- volume
- 24
- issue
- 1-2
- pages
- 31 - 37
- publisher
- Taylor & Francis
- conference name
- Sixth Carbohydrate Bioengineering Meeting
- conference location
- Barcelona, Spain
- conference dates
- 2005-04-03 - 2005-04-06
- external identifiers
-
- wos:000239089700005
- scopus:33646838036
- ISSN
- 1024-2422
- 1029-2446
- DOI
- 10.1080/10242420500518516
- project
- Designed carbohydrate binding modules and molecular probes
- language
- English
- LU publication?
- yes
- id
- 6bd9f891-d050-40fd-b68f-05779f82ca8d (old id 401453)
- date added to LUP
- 2016-04-01 12:02:02
- date last changed
- 2024-06-18 06:09:07
@inproceedings{6bd9f891-d050-40fd-b68f-05779f82ca8d,
abstract = {{Structure-function studies are frequently practiced on the very diverse group of natural carbohydrate-binding modules in order to understand the target recognition of these proteins. We have taken a step further in the study of carbohydrate-binding modules and created variants with novel binding properties by molecular engineering of one such molecule of known 3D-structure. A combinatorial library was created from the sequence encoding a thermostable carbohydrate-binding module, CBM4-2 from a Rhodothermus marinus xylanase, and phage-display technology was successfully used for selection of variants with specificity towards different carbohydrate polymers (birchwood xylan, Avicel (TM), ivory nut mannan and recently also xyloglucan), as well as towards a glycoprotein (human IgG4). Our work not only generated a number of binders with properties that would suite a range of biotechnological applications, but analysis of selected binders also helped us to identify residues important for their specificities.}},
author = {{Cicortas Gunnarsson, Lavinia and Nordberg Karlsson, Eva and Andersson, Mats and Holst, Olle and Ohlin, Mats}},
booktitle = {{Biocatalysis and Biotransformation}},
issn = {{1024-2422}},
keywords = {{carbohydrate-binding module; binding specificity; combinatorial; library; molecular engineering; phage-display; protein scaffold}},
language = {{eng}},
number = {{1-2}},
pages = {{31--37}},
publisher = {{Taylor & Francis}},
title = {{Molecular engineering of a thermostable carbohydrate-binding module}},
url = {{http://dx.doi.org/10.1080/10242420500518516}},
doi = {{10.1080/10242420500518516}},
volume = {{24}},
year = {{2006}},
}