Expression and Purification of Recombinant Duck Ovalbumin in Escherichia coli
- 1Department of Biology, Faculty of Mathematics and Natural Sciences, Bogor Agricultural University (IPB University), IPB Dramaga Campus, Bogor City 16680, Indonesia
- 2Department of Biology, Faculty of Mathematics and Natural Sciences, Bogor Agricultural University (IPB University), IPB Dramaga Campus, Bogor City 16680, Indonesia. Biotechnology Research Center, Bogor Agricultural University (IPB University), IPB Dramaga Campus, Bogor City 16680, Indonesia
Abstract
Ovalbumin (OVA) is a major egg white protein with a balanced amino acid profile and high digestibility, making it valuable for pharmaceutical, nutritional, and health applications. Recombinant production of ovalbumin provides a sustainable and consistent protein source that may reduce allergenic risks and offer alternatives suitable for vegetarian consumers. This study aimed to express duck ovalbumin protein in Escherichia coli as an alternative protein source. Total mRNA was isolated from duck ovarian tissue, reverse-transcribed into cDNA, and the OVA coding sequence was cloned from pGEMT-OVA into the pET28a expression vector. The constructed vector was transformed into E. coli BL21 (DE3) pLysS and E. coli (DE3) Rosetta strains. Recombinant ovalbumin was successfully expressed with an estimated molecular weight of ~45 kDa. Optimal protein production was achieved with induction using 0.25 mM isopropyl-β-D-1-thiogalactopyranoside (IPTG). Purification steps were required to isolate recombinant ovalbumin from host proteins, confirming the feasibility of microbial systems for sustainable OVA production.
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BibTeX
@article{therese2026expression,
title = {{Expression and Purification of Recombinant Duck Ovalbumin in Escherichia coli}},
author = {Miryam Madeleine Therese and Antonius Suwanto and Nisa Rachmania Mubarik},
journal = {Hayati Journal of Biosciences},
year = {2026},
month = oct,
doi = {10.4308/hjb.33.6.1552-1563},
url = {https://doi.org/10.4308/hjb.33.6.1552-1563},
note = {CC BY-NC},
}
RIS
TY - JOUR
TI - Expression and Purification of Recombinant Duck Ovalbumin in Escherichia coli
AU - Miryam Madeleine Therese
AU - Antonius Suwanto
AU - Nisa Rachmania Mubarik
PY - 2026
DA - 2026/10/30
JO - Hayati Journal of Biosciences
DO - 10.4308/hjb.33.6.1552-1563
UR - https://doi.org/10.4308/hjb.33.6.1552-1563
AB - Ovalbumin (OVA) is a major egg white protein with a balanced amino acid profile and high digestibility, making it valuable for pharmaceutical, nutritional, and health applications. Recombinant production of ovalbumin provides a sustainable and consistent protein source that may reduce allergenic risks and offer alternatives suitable for vegetarian consumers. This study aimed to express duck ovalbumin protein in Escherichia coli as an alternative protein source. Total mRNA was isolated from duck ovarian tissue, reverse-transcribed into cDNA, and the OVA coding sequence was cloned from pGEMT-OVA into the pET28a expression vector. The constructed vector was transformed into E. coli BL21 (DE3) pLysS and E. coli (DE3) Rosetta strains. Recombinant ovalbumin was successfully expressed with an estimated molecular weight of ~45 kDa. Optimal protein production was achieved with induction using 0.25 mM isopropyl-β-D-1-thiogalactopyranoside (IPTG). Purification steps were required to isolate recombinant ovalbumin from host proteins, confirming the feasibility of microbial systems for sustainable OVA production.
SN - 1978-3019
SN - 2086-4094
ER -