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Karakteristik fungsional hidrolisat kolagen kulit tuna yang dihidrolisis dengan pepsin dari lambung tuna: Functional characteristics of tuna skin collagen hydrolyzed by tuna gastric pepsin

Functional characteristics of tuna skin collagen hydrolyzed by tuna gastric pepsin: Functional characteristics of tuna skin collagen hydrolyzed by tuna gastric pepsin

Jurnal Pengolahan Hasil Perikanan Indonesia · Vol. 29 No. 5 (2026)

DOI
10.17844/6606j042
ISSN
2354-886X, 2303-2111
Published
2026-06-17
Publisher
Department of Aquatic Product Technology IPB University in collaboration with Masyarakat Pengolahan Hasil Perikanan Indonesia (MPHPI)
Language
ind
License
creativecommons.org/licenses/by/4.0

Abstract

Indonesian

Hidrolisis kolagen dapat dilakukan menggunakan metode ekstraksi pelarut, degradasi kimia, fermentasi dan enzimatik. Produk hidrolisat yang dihidrolisis menggunakan enzim, memiliki peptida bioaktif yang bermanfaat bagi kesehatan. Motif spesifik yang dihasilkan dalam proses hidrolisis misalnya urutan prolina/hidroksiprolina dan glisina, atau prolina di C-terminus sering dikaitkan dengan bioaktivitas inhibisi ACE atau efek antioksidan. Hidrolisat dapat diproduksi dengan bahan baku hasil samping produk perikanan berupa kulit ikan tuna sirip kuning sebagai kolagen dan lambung tuna sebagai sumber pepsin penghidrolisis kolagen. Penelitian bertujuan menentukan aktivitas pepsin dan suhu hidrolisis terbaik dalam menghasilkan hidrolisat kolagen yang dihidrolisis pepsin lambung tuna. Penelitian terdiri dari 2 tahap, yaitu ekstraksi pepsin dari lambung ikan tuna sirip kuning dan pembuatan hidrolisat kolagen secara enzimatis menggunakan enzim pepsin. Aktivitas yang digunakan, yaitu 6.000, 9.000 dan 12.000 U dan suhu 40, 50 dan 60. Ekstrak pepsin yang diperoleh memiliki aktivitas sebesar 12.332 U/mg. Uji aktivitas antioksidan ABTS diperoleh nilai IC50 paling baik pada perlakuan hidrolisis suhu 50ºC, dengan nilai yang diperoleh perlakuan 6.000 U sebesar 109 ppm, perlakuan 9.000 U sebesar 59 ppm, dan perlakuan 12.000 U sebesar 230 ppm. Aktivitas antioksidan DPPH diperoleh nilai IC50 paling baik pada perlakuan hidrolisis suhu 40ºC, dengan nilai masing masing 232 ppm,194 ppm, dan 531 ppm. Hidrolisat kolagen pada konsentrasi 1,7 mg/mL protein setiap perlakuannya, memperoleh nilai inhibisi pada rentang 40-66%.

English

Collagen hydrolysis can be performed using solvent extraction, chemical degradation, fermentation, and enzymatic methods, among others. Hydrolysates produced using enzymes contain bioactive peptides that are beneficial for health. Specific motifs produced during hydrolysis, such as prolinae/hydroxyprolinae and glycine sequences, or prolinae at the C-terminus, are often associated with ACE-inhibitory bioactivity or antioxidant effects. Hydrolysates can be produced using byproducts of the fisheries industry, such as yellowfin tuna skin as a source of collagen and tuna stomach as a source of collagen-hydrolyzing pepsin. This study aimed to identify the optimal pepsin activity and hydrolysis temperature for producing collagen hydrolysate using pepsin derived from tuna stomach. The research was conducted in two stages: extraction of pepsin from the stomach of yellowfin tuna and production of enzymatic collagen hydrolysate using pepsin. The activities tested were 6,000, 9,000, and 12,000 U, with temperatures set at 40, 50, and 60°C. The extracted pepsin exhibited an activity of 12,332 U/mg pepsin. The ABTS antioxidant activity test revealed that the best IC50 value was achieved during hydrolysis at 50 °C, with values of 109 ppm for the 6,000 U treatment, 59 ppm for the 9,000 U treatment, and 230 ppm for the 12,000 U treatment. The most favorable IC50 value for DPPH antioxidant activity was observed during hydrolysis at 40°C, with respective values of 232, 194, and 531 ppm. Collagen hydrolysates at a concentration of 1.7 mg/mL of protein in each treatment showed inhibition values in the range of 40–66%.

Keywords

Collaboration network of the authors

40 authors · 152 co-authorship links · 1 across different organisations · showing the 40 most connected

Hover or tap a name to highlight its co-authors. Double-click to open the author's page.

  • IPB University
  • Bandung Institute of Technology
  • State University of Gorontalo
  • Affiliation unknown
  • Different organisations
  • Same organisation
  • Affiliation unknown
  • Thicker line = more joint articles · bigger circle = more articles
Show as table
Co-authorOrganisationJoint articles
nurjanah nurjanahAffiliation unknown20
Mala NurilmalaAffiliation unknown16
Wini TrilaksaniIPB University6
Roni NugrahaAffiliation unknown6
Ella SalamahAffiliation unknown5
MAGGY T. SUHARTONOAffiliation unknown5
NurjanahAffiliation unknown5
Puji RiantiAffiliation unknown4
Agoes Mardiono JacoebAffiliation unknown4
Pipih SuptijahIPB University4
Ruddy SuwandiAffiliation unknown4
Anggrei Viona SeulalaeAffiliation unknown4
Bambang RiyantoBandung Institute of Technology3
Bustami IbrahimAffiliation unknown3
DesniarAffiliation unknown3
Untung Trimo LaksonoAffiliation unknown3
Raden Hilman WirayudhaAffiliation unknown3
Shindy Hamidah ManteuAffiliation unknown3
Agoes Mardiono JacoebAffiliation unknown3
Rizsa Mustika PertiwiAffiliation unknown3
Gian PrimahanaAffiliation unknown3
Desniar DesniarAffiliation unknown2
Joko SantosoAffiliation unknown2
Silva FauziahAffiliation unknown2
Ace BaehakiAffiliation unknown2
medal lintas percekaAffiliation unknown2
Sri PurwaningsihAffiliation unknown2
Sugeng Heri SusenoIPB University2
N. NurjanahAffiliation unknown2
Giri Rohmad BarokahAffiliation unknown2
Chairun NufusAffiliation unknown2
Uju UjuAffiliation unknown2
Evira LisnainaAffiliation unknown2
Roza YusfiandayaniAffiliation unknown1
M. Fedi A. SonditaAffiliation unknown1
Reinal PutalanState University of Gorontalo1
Ekowati ChasanahAffiliation unknown1

Affiliations come from OpenAlex; journal OAI-PMH metadata carries none. Authors without an OpenAlex ID are matched by name, which can merge or split people.

Metadata source: OAI-PMH (metadata jurnal) http://journal.ipb.ac.id/index.php/jphpi/oai, first harvested 9 Nov 2026, last seen 9 Nov 2026.
Original metadata (oai_dc)
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	<dc:title xml:lang="en">Karakteristik fungsional hidrolisat kolagen kulit tuna yang dihidrolisis dengan pepsin dari lambung tuna: Functional characteristics of tuna skin collagen hydrolyzed by tuna gastric pepsin</dc:title>
	<dc:title xml:lang="id">Functional characteristics of tuna skin collagen hydrolyzed by tuna gastric pepsin: Functional characteristics of tuna skin collagen hydrolyzed by tuna gastric pepsin</dc:title>
	<dc:creator xml:lang="en">Muttaqin, Roisul Adi Brilianto</dc:creator>
	<dc:creator xml:lang="en">Abdullah, Asadatun </dc:creator>
	<dc:creator xml:lang="id">Muttaqin, Roisul Adi Brilianto</dc:creator>
	<dc:creator xml:lang="id">Tati Nurhayati</dc:creator>
	<dc:creator xml:lang="id">Abdullah, Asadatun </dc:creator>
	<dc:subject xml:lang="en">ACE inhibitor</dc:subject>
	<dc:subject xml:lang="en">antioxidant</dc:subject>
	<dc:subject xml:lang="en">degree of hydrolysis</dc:subject>
	<dc:subject xml:lang="en">molecular weight</dc:subject>
	<dc:subject xml:lang="en">peptide</dc:subject>
	<dc:subject xml:lang="id">antioksidan</dc:subject>
	<dc:subject xml:lang="id">bobot molekul</dc:subject>
	<dc:subject xml:lang="id">derajat hidrolisis</dc:subject>
	<dc:subject xml:lang="id">inhibitor ACE</dc:subject>
	<dc:subject xml:lang="id">peptida</dc:subject>
	<dc:description xml:lang="id">Hidrolisis kolagen dapat dilakukan menggunakan metode ekstraksi pelarut, degradasi kimia, fermentasi dan enzimatik. Produk hidrolisat yang dihidrolisis menggunakan enzim, memiliki peptida bioaktif yang bermanfaat bagi kesehatan. Motif spesifik yang dihasilkan dalam proses hidrolisis misalnya urutan prolina/hidroksiprolina dan glisina, atau prolina di C-terminus sering dikaitkan dengan bioaktivitas inhibisi ACE atau efek antioksidan. Hidrolisat dapat diproduksi dengan bahan baku hasil samping produk perikanan berupa kulit ikan tuna sirip kuning sebagai kolagen dan lambung tuna sebagai sumber pepsin penghidrolisis kolagen. Penelitian bertujuan menentukan aktivitas pepsin dan suhu hidrolisis terbaik dalam menghasilkan hidrolisat kolagen yang dihidrolisis pepsin lambung tuna. Penelitian terdiri dari 2 tahap, yaitu ekstraksi pepsin dari lambung ikan tuna sirip kuning dan pembuatan hidrolisat kolagen secara enzimatis menggunakan enzim pepsin. Aktivitas yang digunakan, yaitu 6.000, 9.000 dan 12.000 U dan suhu 40, 50 dan 60. Ekstrak pepsin yang diperoleh memiliki aktivitas sebesar 12.332 U/mg. Uji aktivitas antioksidan ABTS diperoleh nilai IC50 paling baik pada perlakuan hidrolisis suhu 50ºC, dengan nilai yang diperoleh perlakuan 6.000 U sebesar 109 ppm, perlakuan 9.000 U sebesar 59 ppm, dan perlakuan 12.000 U sebesar 230 ppm. Aktivitas antioksidan DPPH diperoleh nilai IC50 paling baik pada perlakuan hidrolisis suhu 40ºC, dengan nilai masing masing 232 ppm,194 ppm, dan 531 ppm. Hidrolisat kolagen pada konsentrasi 1,7 mg/mL protein setiap perlakuannya, memperoleh nilai inhibisi pada rentang 40-66%.</dc:description>
	<dc:description xml:lang="en">Collagen hydrolysis can be performed using solvent extraction, chemical degradation, fermentation, and enzymatic methods, among others. Hydrolysates produced using enzymes contain bioactive peptides that are beneficial for health. Specific motifs produced during hydrolysis, such as prolinae/hydroxyprolinae and glycine sequences, or prolinae at the C-terminus, are often associated with ACE-inhibitory bioactivity or antioxidant effects. Hydrolysates can be produced using byproducts of the fisheries industry, such as yellowfin tuna skin as a source of collagen and tuna stomach as a source of collagen-hydrolyzing pepsin. This study aimed to identify the optimal pepsin activity and hydrolysis temperature for producing collagen hydrolysate using pepsin derived from tuna stomach. The research was conducted in two stages: extraction of pepsin from the stomach of yellowfin tuna and production of enzymatic collagen hydrolysate using pepsin. The activities tested were 6,000, 9,000, and 12,000 U, with temperatures set at 40, 50, and 60°C. The extracted pepsin exhibited an activity of 12,332 U/mg pepsin. The ABTS antioxidant activity test revealed that the best IC50 value was achieved during hydrolysis at 50 °C, with values of 109 ppm for the 6,000 U treatment, 59 ppm for the 9,000 U treatment, and 230 ppm for the 12,000 U treatment. The most favorable IC50 value for DPPH antioxidant activity was observed during hydrolysis at 40°C, with respective values of 232, 194, and 531 ppm. Collagen hydrolysates at a concentration of 1.7 mg/mL of protein in each treatment showed inhibition values in the range of 40–66%.</dc:description>
	<dc:publisher xml:lang="en">Department of Aquatic Product Technology IPB University in collaboration with Masyarakat Pengolahan Hasil Perikanan Indonesia (MPHPI)</dc:publisher>
	<dc:date>2026-06-17</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>
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	<dc:format>text/xml</dc:format>
	<dc:identifier>https://journal.ipb.ac.id/jphpi/article/view/70126</dc:identifier>
	<dc:identifier>10.17844/6606j042</dc:identifier>
	<dc:source xml:lang="id">Jurnal Pengolahan Hasil Perikanan Indonesia; Vol 29 No 5 (2026): Jurnal Pengolahan Hasil Perikanan Indonesia 29(5)</dc:source>
	<dc:source xml:lang="en">Jurnal Pengolahan Hasil Perikanan Indonesia; Vol. 29 No. 5 (2026): Jurnal Pengolahan Hasil Perikanan Indonesia 29(5)</dc:source>
	<dc:source>2354-886X</dc:source>
	<dc:source>2303-2111</dc:source>
	<dc:language>ind</dc:language>
	<dc:relation>https://journal.ipb.ac.id/jphpi/article/view/70126/33531</dc:relation>
	<dc:relation>https://journal.ipb.ac.id/jphpi/article/view/70126/34129</dc:relation>
	<dc:rights xml:lang="en">Copyright (c) 2026 Roisul Adi Brilianto Muttaqin, Tati Nurhayati, Asadatun Abdullah</dc:rights>
	<dc:rights xml:lang="en">https://creativecommons.org/licenses/by/4.0</dc:rights>
</oai_dc:dc>