Abstract
Cellulosomal systems are known as highly efficient biocatalysts in the degradation of lignocellulosic biomass in nature, but they remain unsuitable for industrial applications. In seeking alternatives to natural cellulosomes, casein was chosen as a scaffold for cellulase clustering. Casein is recognized as an excellent substrate for microbial transglutaminase (MTG) because it contains naturally reactive glutamine and lysine residues. A substrate peptide containing an MTG-reactive lysine residue was inserted into the C-terminus of the endoglucanase Cel5A and Cel6A from Thermobifida fusca using genetic engineering. The engineered cellulases, EG(Cel5A) and EG(Cel6A), were conjugated onto casein in different ratios by an MTG-mediated site-specific protein crosslinking reaction. Overall, a more than two-fold increase was observed when EG(Cel5A) was conjugated onto N,N-dimethylcasein, but a small or no change was observed for EG(Cel6A).
| Original language | English |
|---|---|
| Pages (from-to) | 140-145 |
| Number of pages | 6 |
| Journal | Process Biochemistry |
| Volume | 66 |
| DOIs | |
| Publication status | Published - Mar 2018 |
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All Science Journal Classification (ASJC) codes
- Bioengineering
- Biochemistry
- Applied Microbiology and Biotechnology
Cite this
Casein-based scaffold for artificial cellulosome design. / Budinova, Geisa A.L.G.; Mori, Yutaro; Tanaka, Tsutomu; Kamiya, Noriho.
In: Process Biochemistry, Vol. 66, 03.2018, p. 140-145.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Casein-based scaffold for artificial cellulosome design
AU - Budinova, Geisa A.L.G.
AU - Mori, Yutaro
AU - Tanaka, Tsutomu
AU - Kamiya, Noriho
PY - 2018/3
Y1 - 2018/3
N2 - Cellulosomal systems are known as highly efficient biocatalysts in the degradation of lignocellulosic biomass in nature, but they remain unsuitable for industrial applications. In seeking alternatives to natural cellulosomes, casein was chosen as a scaffold for cellulase clustering. Casein is recognized as an excellent substrate for microbial transglutaminase (MTG) because it contains naturally reactive glutamine and lysine residues. A substrate peptide containing an MTG-reactive lysine residue was inserted into the C-terminus of the endoglucanase Cel5A and Cel6A from Thermobifida fusca using genetic engineering. The engineered cellulases, EG(Cel5A) and EG(Cel6A), were conjugated onto casein in different ratios by an MTG-mediated site-specific protein crosslinking reaction. Overall, a more than two-fold increase was observed when EG(Cel5A) was conjugated onto N,N-dimethylcasein, but a small or no change was observed for EG(Cel6A).
AB - Cellulosomal systems are known as highly efficient biocatalysts in the degradation of lignocellulosic biomass in nature, but they remain unsuitable for industrial applications. In seeking alternatives to natural cellulosomes, casein was chosen as a scaffold for cellulase clustering. Casein is recognized as an excellent substrate for microbial transglutaminase (MTG) because it contains naturally reactive glutamine and lysine residues. A substrate peptide containing an MTG-reactive lysine residue was inserted into the C-terminus of the endoglucanase Cel5A and Cel6A from Thermobifida fusca using genetic engineering. The engineered cellulases, EG(Cel5A) and EG(Cel6A), were conjugated onto casein in different ratios by an MTG-mediated site-specific protein crosslinking reaction. Overall, a more than two-fold increase was observed when EG(Cel5A) was conjugated onto N,N-dimethylcasein, but a small or no change was observed for EG(Cel6A).
UR - http://www.scopus.com/inward/record.url?scp=85042087173&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85042087173&partnerID=8YFLogxK
U2 - 10.1016/j.procbio.2017.12.013
DO - 10.1016/j.procbio.2017.12.013
M3 - Article
AN - SCOPUS:85042087173
VL - 66
SP - 140
EP - 145
JO - Process Biochemistry
JF - Process Biochemistry
SN - 0032-9592
ER -