Melola Discovery

← Melola Discovery

Akses terbuka Jurnal SINTA 1

Expression and Purification of Recombinant Duck Ovalbumin in Escherichia coli

HAYATI Journal of Biosciences · Vol. 33 No. 6 (2026) · hlm. 1552–1563

DOI
10.4308/hjb.33.6.1552-1563
ISSN
2086-4094, 1978-3019
Terbit
2026-11-01
Penerbit
Bogor Agricultural University, Indonesia
Bahasa
eng
Lisensi
creativecommons.org/licenses/by-nc/4.0

Abstrak

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.

Jaringan kolaborasi para penulis

40 penulis · 98 tautan kepenulisan bersama · 19 lintas organisasi · menampilkan 40 yang paling banyak terhubung

Arahkan kursor atau ketuk sebuah nama untuk menyorot rekan penulisnya. Klik dua kali untuk membuka halaman penulis.

  • IPB University
  • Universitas Sumatera Utara
  • University of Bengkulu
  • University of Indonesia
  • Universitas Pattimura
  • Montana State University
  • State University of Makassar
  • Organisasi lain
  • Afiliasi tidak diketahui
  • Organisasi berbeda
  • Organisasi sama
  • Afiliasi tidak diketahui
  • Garis lebih tebal = lebih banyak artikel bersama · lingkaran lebih besar = lebih banyak artikel
Tampilkan sebagai tabel
Rekan penulisOrganisasiArtikel bersama
Aris Tri WahyudiIPB University8
İman RusmanaIPB University8
Esti PuspitasariIPB University5
Andreas Adhi SatyaAfiliasi tidak diketahui4
Rika Indri AstutiIPB University4
Dwi SuryantoUniversitas Sumatera Utara3
Anja MeryandiniIPB University3
Laksmi AmbarsariIPB University2
Risky Hadi WibowoAfiliasi tidak diketahui2
Sipriyadi SipriyadiUniversity of Bengkulu2
Widanarni WidanarniIPB University2
Amarila MalikUniversity of Indonesia2
Bibiana W. LayIPB University2
Sri BudiartiIPB University2
Yulin LestariIPB University2
Dedy Duryadi SolihinIPB University2
Cecilia Anna SeumahuUniversitas Pattimura2
Maria Indah PurnamasariMontana State University2
Yepy H. RustamAfiliasi tidak diketahui2
Sakina Maya MaulawiIPB University1
Siti Azzira RahmaIPB University1
Lisdar A ManafIPB University1
Maggy Thenawidjaya SuhartonoIPB University1
Iah Novi MaslahahIPB University1
Nurul AiniIPB University1
Walter R. ErdelenIPB University1
Muhammad ZairinIPB University1
Ridwan AffandiIPB University1
Yusminah HalaState University of Makassar1
Sukenda SukendaIPB University1
Budi TjahjonoIPB University1
R. HarlingScottish Agricultural College1
Budiasih WahyuntariAfiliasi tidak diketahui1
Marita AnggaraniIPB University1
SumardiAfiliasi tidak diketahui1
Maggy T HenawidjajaIPB University1
T Resnawati P UrwadariaAfiliasi tidak diketahui1

Afiliasi berasal dari OpenAlex; metadata OAI-PMH jurnal tidak memuatnya. Penulis tanpa ID OpenAlex dicocokkan berdasarkan nama, sehingga dua orang bisa tergabung atau satu orang bisa terpisah.

Sumber metadata: OAI-PMH (metadata jurnal) http://journal.ipb.ac.id/index.php/hayati/oai, pertama di-harvest 8 Nov 2026, terakhir terlihat 8 Nov 2026.
Metadata asli (oai_dc) 
<oai_dc:dc xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/  http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
	<dc:title xml:lang="en">Expression and Purification of Recombinant Duck Ovalbumin in Escherichia coli</dc:title>
	<dc:creator xml:lang="en">Therese, Miryam Madeleine</dc:creator>
	<dc:creator xml:lang="en">Suwanto, Antonius</dc:creator>
	<dc:creator xml:lang="en">Mubarik, Nisa Rachmania</dc:creator>
	<dc:description xml:lang="en">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.</dc:description>
	<dc:publisher xml:lang="en">Bogor Agricultural University, Indonesia</dc:publisher>
	<dc:date>2026-11-01</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:type xml:lang="en">Peer-reviewed Article</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>http://journal.ipb.ac.id/hayati/article/view/69953</dc:identifier>
	<dc:identifier>10.4308/hjb.33.6.1552-1563</dc:identifier>
	<dc:source xml:lang="en">HAYATI Journal of Biosciences; Vol. 33 No. 6 (2026): November 2026; 1552-1563</dc:source>
	<dc:source>2086-4094</dc:source>
	<dc:source>1978-3019</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>http://journal.ipb.ac.id/hayati/article/view/69953/34542</dc:relation>
	<dc:rights xml:lang="en">Copyright (c) 2026 Miryam Madeleine Therese, Antonius Suwanto, Nisa Rachmania Mubarik</dc:rights>
	<dc:rights xml:lang="en">https://creativecommons.org/licenses/by-nc/4.0</dc:rights>
</oai_dc:dc>