Melola Discovery

← Melola Discovery

Jurnal SINTA 1

Extraction of Collagen from the Skin of Kacang Goat and Production of Its Hydrolysate as an Inhibitor of Angiotensin Converting Enzyme

Tropical Animal Science Journal · Vol. 44 No. 2 (2021) · hlm. 222–228

DOI
10.5398/tasj.2021.44.2.222
ISSN
2615-790X, 2615-787X
Terbit
2021-06-01
Penerbit
Faculty of Animal Science, IPB University
Bahasa
eng

Abstrak

The study was designed to determine the potential of collagen hydrolysate produced from the skin of Kacang goat through chymotrypsin hydrolysis to be used as an inhibitor of angiotensin converting enzyme (ACE). This research was conducted in three replications, with the measured parameters include ACE inhibitory potential and collagen hydrolysate fractionation. The results showed that collagen extraction of Kacang goat skin by chymotrypsin hydrolysis yielded 9.74% (dry matter, v/v) collagen, with pH at 6.6. The extracted collagen contained α1, α2, and β collagen chains with molecular weights of 151 kDa, 141 kDa, and 240 kDa, respectively. Furthermore, the collagen hydrolysis produced protein peptides confirmed at molecular weights of 43 to 107 kDa. The hydrolysate fractionation at molecular weights of 5 kDa showed proteins concentrations of 2.33 mg/mL, 3.81 mg/mL, and 3.93 mg/mL, respectively. The hydrolysate fractionation with molecular weight <3 kDa showed to have ACE inhibition activity with the IC50 value of 0.47 mg/mL. The study concluded that collagen hydrolysate extracted from the skin of Kacang goat had a promising potential as a source of antihypertensive agent.

Kata kunci

Jaringan kolaborasi para penulis

40 penulis · 125 tautan kepenulisan bersama · 45 lintas organisasi

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

  • Universitas Gadjah Mada
  • Universitas Jember
  • Politeknik ATK Yogyakarta
  • National Research and Innovation Agency
  • Hasanuddin University
  • Padjadjaran University
  • Politeknik Negeri Jember
  • 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
Anggia Risty AmaryllisUniversitas Gadjah Mada2
Almira Tsania AflahUniversitas Gadjah Mada2
Nur VeraUniversitas Gadjah Mada2
Dicky Tri UtamaPadjadjaran University2
Yudi PranotoUniversitas Gadjah Mada2
Dwi WulandariPoliteknik ATK Yogyakarta2
Ragil YuliatmoPoliteknik ATK Yogyakarta2
MuhlisinPoliteknik Ilmu Pelayaran Makassar2
WihandoyoAfiliasi tidak diketahui2
Bangkit Lutfiaji SyaefullahUniversitas Gadjah Mada2
Ragil Adi PrasetyoUniversitas Gadjah Mada2
Novita KurniawatiUniversitas Gadjah Mada2
Muhammad Irfan SaidHasanuddin University1
Suharjono TriatmojoAfiliasi tidak diketahui1
Achmad FudholiAfiliasi tidak diketahui1
Kahpiana KahpianaAfiliasi tidak diketahui1
Sri HartatikUniversitas Jember1
Edi SuryantoUniversitas Gadjah Mada1
Joni Murti Mulyo AjiUniversitas Jember1
Agus Hadi PrayitnoPoliteknik Negeri Jember1
Tri Agus SiswoyoUniversitas Gadjah Mada1
T LindriantiUniversitas Gadjah Mada1
Rusman RusmanUniversitas Gadjah Mada1
Chusnul HanimUniversitas Gadjah Mada1
Agung IrawanSebelas Maret University1
Lukita PurnamayantiUniversitas Gadjah Mada1
Abdul RohmanUniversitas Gadjah Mada1
Nor Kartini Abu BakarUniversity of Malaya1
Anjar WindarsihNational Research and Innovation Agency1
Yuniar KhasanahNational Research and Innovation Agency1
NurliyaniAfiliasi tidak diketahui1
Istiti KandarinaUniversitas Gadjah Mada1

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) https://journal.ipb.ac.id/index.php/tasj/oai, pertama di-harvest 10 Nov 2026, terakhir terlihat 10 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">Extraction of Collagen from the Skin of Kacang Goat and Production of Its Hydrolysate as an Inhibitor of Angiotensin Converting Enzyme</dc:title>
	<dc:creator xml:lang="en">Hakim, T. R.</dc:creator>
	<dc:creator xml:lang="en">Pratiwi, A.</dc:creator>
	<dc:creator xml:lang="en">Jamhari, Jamhari</dc:creator>
	<dc:creator xml:lang="en">Fitriyanto, N. A.</dc:creator>
	<dc:creator xml:lang="en">Rusman, Rusman</dc:creator>
	<dc:creator xml:lang="en">Abidin, M. Z.</dc:creator>
	<dc:creator xml:lang="en">Matulessy, D. N.</dc:creator>
	<dc:creator xml:lang="en">Erwanto, Y.</dc:creator>
	<dc:subject xml:lang="en">antihypertensive</dc:subject>
	<dc:subject xml:lang="en">chymotrypsin</dc:subject>
	<dc:subject xml:lang="en">collagen of goat skin</dc:subject>
	<dc:subject xml:lang="en">hydrolysate</dc:subject>
	<dc:subject xml:lang="en">IC50</dc:subject>
	<dc:description xml:lang="en">The study was designed to determine the potential of collagen hydrolysate produced from the skin of Kacang goat through chymotrypsin hydrolysis to be used as an inhibitor of angiotensin converting enzyme (ACE). This research was conducted in three replications, with the measured parameters include ACE inhibitory potential and collagen hydrolysate fractionation. The results showed that collagen extraction of Kacang goat skin by chymotrypsin hydrolysis yielded 9.74% (dry matter, v/v) collagen, with pH at 6.6. The extracted collagen contained α1, α2, and β collagen chains with molecular weights of 151 kDa, 141 kDa, and 240 kDa, respectively. Furthermore, the collagen hydrolysis produced protein peptides confirmed at molecular weights of 43 to 107 kDa. The hydrolysate fractionation at molecular weights of &amp;lt;3 kDa, 3-5 kDa, and &amp;gt;5 kDa showed proteins concentrations of 2.33 mg/mL, 3.81 mg/mL, and 3.93 mg/mL, respectively. The hydrolysate fractionation with molecular weight &amp;lt;3 kDa showed to have ACE inhibition activity with the IC50 value of 0.47 mg/mL. The study concluded that collagen hydrolysate extracted from the skin of Kacang goat had a promising potential as a source of antihypertensive agent.</dc:description>
	<dc:publisher xml:lang="en">Faculty of Animal Science, IPB University</dc:publisher>
	<dc:date>2021-06-01</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://journal.ipb.ac.id/tasj/article/view/32160</dc:identifier>
	<dc:identifier>10.5398/tasj.2021.44.2.222</dc:identifier>
	<dc:source xml:lang="en">Tropical Animal Science Journal; Vol. 44 No. 2 (2021): Tropical Animal Science Journal; 222-228</dc:source>
	<dc:source>2615-790X</dc:source>
	<dc:source>2615-787X</dc:source>
	<dc:source>10.5398/tasj.2021.44.2</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://journal.ipb.ac.id/tasj/article/view/32160/21704</dc:relation>
	<dc:rights xml:lang="en">Copyright (c) 2021 Tropical Animal Science Journal</dc:rights>
</oai_dc:dc>