Abstract
The recombinant tyrosinase from Verrucomicrobium spinosum bacteria has been obtained by heterologous expression in E. coli and isolated in the pure state to determine some of its biochemical properties (the kinetics of the enzymatic reaction, the effect of an inhibitor and activator, and the pH optimum). Coexpression of the genes for tyrosinase and recombinant adhesive mussel protein in one producer strain was used to introduce posttranslational modifications into the adhesive protein. These modifications involved the transformation of tyrosine residues into DOPA residues, which makes the protein capable of molecular adhesion in an aqueous medium.
| Original language | English |
|---|---|
| Pages (from-to) | 780-792 |
| Number of pages | 13 |
| Journal | Applied Biochemistry and Microbiology |
| Volume | 54 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Dec 1 2018 |
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Keywords
- adhesion strength
- adhesive protein
- biocompatible glue
- DOPA
- enzymatic activity
- tyrosinase
ASJC Scopus subject areas
- Biochemistry
- Applied Microbiology and Biotechnology
Cite this
Recombinant Tyrosinase from Verrucomicrobium spinosum : Isolation, Characteristics, and Use for the Production of a Protein with Adhesive Properties. / Aksambayeva, A. S.; Zhaparova, L. R.; Shagyrova, Zh S.; Zhiyenbay, E.; Nurgozhin, Talgat; Ramankulov, E. M.; Shustov, A. V.
In: Applied Biochemistry and Microbiology, Vol. 54, No. 8, 01.12.2018, p. 780-792.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Recombinant Tyrosinase from Verrucomicrobium spinosum
T2 - Isolation, Characteristics, and Use for the Production of a Protein with Adhesive Properties
AU - Aksambayeva, A. S.
AU - Zhaparova, L. R.
AU - Shagyrova, Zh S.
AU - Zhiyenbay, E.
AU - Nurgozhin, Talgat
AU - Ramankulov, E. M.
AU - Shustov, A. V.
PY - 2018/12/1
Y1 - 2018/12/1
N2 - The recombinant tyrosinase from Verrucomicrobium spinosum bacteria has been obtained by heterologous expression in E. coli and isolated in the pure state to determine some of its biochemical properties (the kinetics of the enzymatic reaction, the effect of an inhibitor and activator, and the pH optimum). Coexpression of the genes for tyrosinase and recombinant adhesive mussel protein in one producer strain was used to introduce posttranslational modifications into the adhesive protein. These modifications involved the transformation of tyrosine residues into DOPA residues, which makes the protein capable of molecular adhesion in an aqueous medium.
AB - The recombinant tyrosinase from Verrucomicrobium spinosum bacteria has been obtained by heterologous expression in E. coli and isolated in the pure state to determine some of its biochemical properties (the kinetics of the enzymatic reaction, the effect of an inhibitor and activator, and the pH optimum). Coexpression of the genes for tyrosinase and recombinant adhesive mussel protein in one producer strain was used to introduce posttranslational modifications into the adhesive protein. These modifications involved the transformation of tyrosine residues into DOPA residues, which makes the protein capable of molecular adhesion in an aqueous medium.
KW - adhesion strength
KW - adhesive protein
KW - biocompatible glue
KW - DOPA
KW - enzymatic activity
KW - tyrosinase
UR - http://www.scopus.com/inward/record.url?scp=85061822538&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85061822538&partnerID=8YFLogxK
U2 - 10.1134/S0003683818080021
DO - 10.1134/S0003683818080021
M3 - Article
VL - 54
SP - 780
EP - 792
JO - Applied Biochemistry and Microbiology
JF - Applied Biochemistry and Microbiology
SN - 0003-6838
IS - 8
ER -