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Ekstraksi dan determinasi karakteristik kolagen gelembung renang ikan lencam (Lethrinus lentjan): Extraction and determination characteristics of swim bladder collagen in pink ear emperor fish (Lethrinus lentjan)

Jurnal Pengolahan Hasil Perikanan Indonesia · Vol. 26 No. 3 (2023)

DOI
10.17844/jphpi.v26i3.45529
ISSN
2354-886X, 2303-2111
Terbit
2023-11-17
Penerbit
Department of Aquatic Product Technology IPB University in collaboration with Masyarakat Pengolahan Hasil Perikanan Indonesia (MPHPI)
Bahasa
ind

Abstrak

Bahasa Indonesia

Ekspor filet ikan lencam yang terus meningkat di Indonesia menyebabkan peningkatan pada jumlah hasil samping produksi, salah satunya gelembung renang. Gelembung renang ikan merupakan sumber alternatif kolagen yang telah menarik minat ilmuwan dan industri untuk diaplikasikan di berbagai sektor kesehatan, farmasi, dan kosmetik. Penelitian ini bertujuan untuk menentukan rasio bahan dan pelarut serta waktu yang optimal pada tahap praperlakuan dalam ekstraksi kolagen dari gelembung renang ikan lencam. Penelitian dibagi menjadi tiga tahapan, yaitu optimasi praperlakuan sampel menggunakan larutan NaOH dengan lama waktu yang berbeda, ekstraksi dengan rasio bahan dan pelarut asam asetat dan penambahan enzim papain, dan karakterisasi kolagen gelembung renang ikan lencam. Analisis komponen gelembung renang ikan lencam meliputi proksimat, asam amino, dan protein terlarut. Analisis kualitas kolagen meliputi proksimat, asam amino, pengukuran warna, derajat putih, pH, pita protein, dan gugus fungsi. Kondisi praperlakuan terbaik didapat pada gelembung renang ikan lencam yang direndam NaOH 0,1 M selama 8 jam. Ekstrasi kolagen gelembung renang ikan lencam terbaik, yaitu rasio 1:30 (b/v) larut enzim papain (PaSC) sebesar 28,88±0,71% selama 48 jam. Kandungan protein mencapai 92,56±0,12%, derajat putih 97,86%, nilai pH 6,64, kandungan hidroksiprolina sebesar 79,32 mg/g, glisina 293,35 mg/g, dan prolina 102,57 mg/g sebagai asam amino penciri kolagen. Hasil deteksi gugus fungsi menunjukkan adanya gugus fungsi amida I, II, III, A, dan B serta rantai α1 dan α2. Pola protein kolagen terdeteksi pada kisaran molekul 100-250 kDa yang mengindikasikan kolagen tipe I.

Inggris

The upswing in the exportation of Lethrinus lentjan fillets in Indonesia has resulted in a concomitant increase in the quantity of production by-products, including swim bladder. Fish swim bladders possess collagen, which has garnered interest from both the scientific and industrial communities for potential applications in healthcare, pharmaceuticals, and cosmetics. The primary objective of this study was to ascertain the most suitable ratio of materials and solvents, as well as the optimal duration of pretreatment, for the effective extraction of collagen from the swim bladders of pink ear emperor fish. The study was conducted in three distinct stages: pretreatment of the sample with NaOH solutions of varying durations, extraction of collagen using papain enzyme and varying ratios of materials and acetic acid, and characterization of the extracted collagen. Examination of the swim bladder constituents of pink ear emperor fish encompasses proximate, amino acid, and dissolved protein analyses. Quality analysis of collagen encompasses various techniques, including proximate analysis, amino acid analysis, color measurement, whiteness degree assessment, pH determination, protein band analysis, and functional group detection. These methods are used to evaluate the chemical and physical properties of collagen, ensuring its purity and suitability for various applications. The optimal pretreatment conditions involved soaking pink ear emperor fish swim bladders in 0.1 M NaOH for 8 h, and the highest yield of collagen was attained using a soluble papain enzyme ratio of 1:30 (w/v) for 48 h, resulting in a collagen output of 28.88±0.71%.The extracted collagen possessed a protein content of 92.56±0.12%, a whiteness degree of 97.86%, a pH value of 6.64, a hydroxyproline content of 79.32 mg/g, a glycine content of 293.35 mg/g, and a proline content of 102.57 mg/g. These values are characteristic of the amino acids found in collagen. The results of functional group detection experimentally confirmed the presence of amide I, II, III, A, and B functional groups, as well as α1 and α2 chains. Collagen protein band analysis identified the presence of collagen type I in the molecular range of 100-250 kDa, as evidenced by the detection of collagen protein patterns in this range.

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  • IPB University
  • Bandung Institute of Technology
  • Politeknik Negeri Pontianak
  • Sriwijaya University
  • Afiliasi tidak diketahui
  • Organisasi berbeda
  • Organisasi sama
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Tampilkan sebagai tabel
Rekan penulisOrganisasiArtikel bersama
Bambang RiyantoIPB University13
Mala NurilmalaIPB University11
Nurjanah NurjanahIPB University10
Asadatun AbdullahIPB University10
Wahyu RamadhanIPB University7
Joko SantosoIPB University7
Asadatun AbdullahIPB University7
Bustami IbrahimIPB University7
Maggy Thenawidjaja SuhartonoIPB University6
Ella SalamahIPB University6
Iriani SetyaningsihIPB University6
Mala NurilmalaAfiliasi tidak diketahui6
Pipih SuptijahIPB University5
Raden Hilman WirayudhaIPB University5
Sugeng Heri SusenoIPB University5
Silva FauziahIPB University5
Uju UjuIPB University5
Kustiariyah TarmanIPB University4
Desniar DesniarIPB University4
Roni NugrahaIPB University4
Wahyu RamadhanAfiliasi tidak diketahui4
Joko SantosoIPB University3
Bambang RiyantoBandung Institute of Technology3
DesniarIPB University3
Untung Trimo LaksonoPoliteknik Negeri Pontianak3
Fahri SinulinggaIPB University3
. UjuAfiliasi tidak diketahui3
NurjanahAfiliasi tidak diketahui3
Ruddy SuwandiIPB University3
Giri Rohmad BarokahIPB University3
Purnama ArafahIPB University3
Safrina Dyah HardiningtyasIPB University3
Farel WidiarsyahIPB University2
Ace BaehakiSriwijaya University2
Sri PurwaningsihIPB University2

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/jphpi/oai, pertama di-harvest 9 Nov 2026, terakhir terlihat 9 Nov 2026.
Metadata asli (oai_dc)
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	<dc:title xml:lang="id">Ekstraksi dan determinasi karakteristik kolagen gelembung renang ikan lencam (Lethrinus lentjan): Extraction and determination characteristics of swim bladder collagen in pink ear emperor fish (Lethrinus lentjan)</dc:title>
	<dc:creator xml:lang="id">Sakinah, Aula </dc:creator>
	<dc:creator xml:lang="id">Trilaksani, Wini </dc:creator>
	<dc:creator xml:lang="id">Nurhayati, Tati </dc:creator>
	<dc:creator xml:lang="en">Sakinah, Aula </dc:creator>
	<dc:creator xml:lang="en">Trilaksani, Wini </dc:creator>
	<dc:creator xml:lang="en">Nurhayati, Tati </dc:creator>
	<dc:subject xml:lang="en">characterization</dc:subject>
	<dc:subject xml:lang="en">collagen</dc:subject>
	<dc:subject xml:lang="en">extraction</dc:subject>
	<dc:subject xml:lang="en">fish swim bladder</dc:subject>
	<dc:subject xml:lang="en">yield</dc:subject>
	<dc:subject xml:lang="id">ekstraksi</dc:subject>
	<dc:subject xml:lang="id">gelembung renang ikan</dc:subject>
	<dc:subject xml:lang="id">karakterisasi</dc:subject>
	<dc:subject xml:lang="id">kolagen</dc:subject>
	<dc:subject xml:lang="id">rendemen</dc:subject>
	<dc:description xml:lang="id">


Ekspor filet ikan lencam yang terus meningkat di Indonesia menyebabkan peningkatan pada jumlah hasil samping produksi, salah satunya gelembung renang. Gelembung renang ikan merupakan sumber alternatif kolagen yang telah menarik minat ilmuwan dan industri untuk diaplikasikan di berbagai sektor kesehatan, farmasi, dan kosmetik. Penelitian ini bertujuan untuk menentukan rasio bahan dan pelarut serta waktu yang optimal pada tahap praperlakuan dalam ekstraksi kolagen dari gelembung renang ikan lencam. Penelitian dibagi menjadi tiga tahapan, yaitu optimasi praperlakuan sampel menggunakan larutan NaOH dengan lama waktu yang berbeda, ekstraksi dengan rasio bahan dan pelarut asam asetat dan penambahan enzim papain, dan karakterisasi kolagen gelembung renang ikan lencam. Analisis komponen gelembung renang ikan lencam meliputi proksimat, asam amino, dan protein terlarut. Analisis kualitas kolagen meliputi proksimat, asam amino, pengukuran warna, derajat putih, pH, pita protein, dan gugus fungsi. Kondisi praperlakuan terbaik didapat pada gelembung renang ikan lencam yang direndam NaOH 0,1 M selama 8 jam. Ekstrasi kolagen gelembung renang ikan lencam terbaik, yaitu rasio 1:30 (b/v) larut enzim papain (PaSC) sebesar 28,88±0,71% selama 48 jam. Kandungan protein mencapai 92,56±0,12%, derajat putih 97,86%, nilai pH 6,64, kandungan hidroksiprolina sebesar 79,32 mg/g, glisina 293,35 mg/g, dan prolina 102,57 mg/g sebagai asam amino penciri kolagen. Hasil deteksi gugus fungsi menunjukkan adanya gugus fungsi amida I, II, III, A, dan B serta rantai α1 dan α2 . Pola protein kolagen terdeteksi pada kisaran molekul 100-250 kDa yang mengindikasikan kolagen tipe I.


</dc:description>
	<dc:description xml:lang="en">


The upswing in the exportation of Lethrinus lentjan fillets in Indonesia has resulted in a concomitant increase in the quantity of production by-products, including swim bladder. Fish swim bladders possess collagen, which has garnered interest from both the scientific and industrial communities for potential applications in healthcare, pharmaceuticals, and cosmetics. The primary objective of this study was to ascertain the most suitable ratio of materials and solvents, as well as the optimal duration of pretreatment, for the effective extraction of collagen from the swim bladders of pink ear emperor fish. The study was conducted in three distinct stages: pretreatment of the sample with NaOH solutions of varying durations, extraction of collagen using papain enzyme and varying ratios of materials and acetic acid, and characterization of the extracted collagen. Examination of the swim bladder constituents of pink ear emperor fish encompasses proximate, amino acid, and dissolved protein analyses. Quality analysis of collagen encompasses various techniques, including proximate analysis, amino acid analysis, color measurement, whiteness degree assessment, pH determination, protein band analysis, and functional group detection. These methods are used to evaluate the chemical and physical properties of collagen, ensuring its purity and suitability for various applications. The optimal pretreatment conditions involved soaking pink ear emperor fish swim bladders in 0.1 M NaOH for 8 h, and the highest yield of collagen was attained using a soluble papain enzyme ratio of 1:30 (w/v) for 48 h, resulting in a collagen output of 28.88±0.71%.The extracted collagen possessed a protein content of 92.56±0.12%, a whiteness degree of 97.86%, a pH value of 6.64, a hydroxyproline content of 79.32 mg/g, a glycine content of 293.35 mg/g, and a proline content of 102.57 mg/g. These values are characteristic of the amino acids found in collagen. The results of functional group detection experimentally confirmed the presence of amide I, II, III, A, and B functional groups, as well as α1 and α2 chains. Collagen protein band analysis identified the presence of collagen type I in the molecular range of 100-250 kDa, as evidenced by the detection of collagen protein patterns in this range.


</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>2023-11-17</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
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	<dc:type xml:lang="en">Peer-reviewed Article</dc:type>
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	<dc:identifier>https://journal.ipb.ac.id/jphpi/article/view/45529</dc:identifier>
	<dc:identifier>10.17844/jphpi.v26i3.45529</dc:identifier>
	<dc:source xml:lang="id">Jurnal Pengolahan Hasil Perikanan Indonesia; Vol 26 No 3 (2023): Jurnal Pengolahan Hasil Perikanan Indonesia 26 (3)</dc:source>
	<dc:source xml:lang="en">Jurnal Pengolahan Hasil Perikanan Indonesia; Vol. 26 No. 3 (2023): Jurnal Pengolahan Hasil Perikanan Indonesia 26 (3)</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/45529/27202</dc:relation>
	<dc:rights xml:lang="en">Copyright (c) 2023 Aula  Sakinah, Wini  Trilaksani, Tati  Nurhayati</dc:rights>
</oai_dc:dc>