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Karakterisasi fraksi amonium sulfat tripsin yang diisolasi dari usus ikan tongkol (Euthynnus affinis): Tripsin dari ikan tongkol

Characterization of Ammonium Sulphate Fraction Tripsin Isolated from Intestine of Little Tuna: Trypsin from little tuna

Jurnal Pengolahan Hasil Perikanan Indonesia · Vol. 23 No. 2 (2020) · pp. 372–382

DOI
10.17844/jphpi.v23i2.32221
ISSN
2354-886X, 2303-2111
Published
2020-09-04
Publisher
Department of Aquatic Product Technology IPB University in collaboration with Masyarakat Pengolahan Hasil Perikanan Indonesia (MPHPI)
Language
ind

Abstract

Indonesian

Usus ikan tongkol merupakan bagian saluran pencernaan ikan yang memiliki pH neteral sehingga berpotensi sebagai sumber enzim, yaitu enzim tripsin. Enzim tripsin dari jeroan ikan bisa menjadi alternatif dari enzim tripsin komersil yang berasal dari babi dan sapi. Penelitian ini bertujuan menganalisis karakteristik fraksi amonium sulfat enzim tripsin dari usus ikan tongkol. Tahapan penelitian diawali dengan ekstraksi enzim tripsin dari usus ikan tongkol lalu difraksinasi menggunakan amonium sulfat (0-80%). Fraksi terbaik dikarakterisasi suhu, pH, pengaruh ion logam, stabilitas terhadap NaCl, dan substrat optimum serta dilakukan analisis kinetika reaksi. Pengukuran aktivitas enzim menggunakan substrat N-α-benzoyl-DL-arginine-p-nitroanilide (BAPNA). Hasil penelitian menunjukkan bahwa ekstrak kasar tripsin memiliki aktivitas sebesar 0,205 U/mL. Aktivitas enzim tripsin tertinggi terdapat pada fraksi amonium sulfat fraksi 40-50% sebesar 0,248 U/mL. Enzim bekerja optimum bekerja pada suhu 60°C dan pH 9. Ion logam ZnCl2 dan CaCl2 menghambat aktivitas tripsin, sedangkan MnCl2, CuCl2, dan NaCl dapat meningkatkan aktivitas tripsin. Aktivitas tripsin stabil pada NaCl 5-30%. Enzim tersebut memiliki nilai Vmaks sebesar 0,42 mmol/s dan nilai Nilai Km sebesar 1,12 mM

English

Intestine is part of the digestive tract of fish having neutral pH. Thus, fish intestine is a potential source of typsin and can be an alternative source to the commercial trypsin enzyme derived from pork and cattle. This study was aimed to analyze the characteristics of the ammonium sulphates fraction of the trypsin enzyme from tuna intestine. The research began with the extraction of the trypsin enzyme from the little tuna intestine and followed up by fractionation using ammonium sulphates (0-80%). Optimum temperature and pH as well as effects of metal ions, stability to NaCl, optimum substrate and reaction kinetics were determined. Enzyme activity was measured using N-α-benzoyl-DL-arginine-p-nitroanilide (BAPNA). The results showed that the trypsin crude extract had an activity of 0.205 U / mL. The highest enzyme activity was found in the ammonium sulphates fraction of 40-50%. The enzyme worked optimally at 60°C and pH 9. Metal ions including ZnCl2 and CaCl2 inhibited trypsin activity, while MnCl2, CuCl2, and NaCl increased trypsin activity. Trypsin activity was stable at 5-30% NaCl. The enzyme had a Vmax value of 0.42 mmol/s and a Km value of 1.12 mM.

Keywords

Collaboration network of the authors

40 authors · 163 co-authorship links · 2 across different organisations · showing the 40 most connected

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  • 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
Mala NurilmalaAffiliation unknown13
Asadatun AbdullahAffiliation unknown10
nurjanah nurjanahAffiliation unknown9
Ruddy SuwandiAffiliation unknown7
Wini TrilaksaniIPB University6
Ella SalamahAffiliation unknown6
MAGGY T. SUHARTONOAffiliation unknown5
Rizsa Mustika PertiwiAffiliation unknown5
Bambang RiyantoBandung Institute of Technology3
Bustami IbrahimAffiliation unknown3
DesniarAffiliation unknown3
Pipih SuptijahIPB University3
Untung Trimo LaksonoAffiliation unknown3
Raden Hilman WirayudhaAffiliation unknown3
Agoes Mardiono JacoebAffiliation unknown3
Sugeng Heri SusenoIPB University3
Desniar DesniarAffiliation unknown2
Joko SantosoAffiliation unknown2
Silva FauziahAffiliation unknown2
Ace BaehakiAffiliation unknown2
medal lintas percekaAffiliation unknown2
Sri PurwaningsihAffiliation unknown2
Giri Rohmad BarokahAffiliation unknown2
Shindy Hamidah ManteuAffiliation unknown2
Uju UjuAffiliation unknown2
Gian PrimahanaAffiliation unknown2
NurjanahAffiliation unknown2
Kustiariyah TarmanIPB University2
Anggrei Viona SeulalaeAffiliation unknown1
Reinal PutalanState University of Gorontalo1
Ekowati ChasanahAffiliation unknown1
Puji RiantiAffiliation unknown1
Agoes Mardiono JacoebAffiliation unknown1
Ari Elisa RatihAffiliation unknown1
Shabrina AuliaAffiliation unknown1
Aninditya Artina SetiaputriAffiliation unknown1
Rahma Dini ArbajayantiAffiliation 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="id">Karakterisasi fraksi amonium sulfat tripsin yang diisolasi dari usus ikan tongkol (Euthynnus affinis): Tripsin dari ikan tongkol</dc:title>
	<dc:title xml:lang="en">Characterization of Ammonium Sulphate Fraction Tripsin Isolated from Intestine of Little Tuna: Trypsin from little tuna</dc:title>
	<dc:creator xml:lang="id">Nurhayati, Tati</dc:creator>
	<dc:creator xml:lang="id">Nugraha, Roni</dc:creator>
	<dc:creator xml:lang="id">Ningdya Lihuana, Diana </dc:creator>
	<dc:creator xml:lang="en">Nurhayati, Tati</dc:creator>
	<dc:creator xml:lang="en">Nugraha, Roni</dc:creator>
	<dc:creator xml:lang="en">Ningdya Lihuana, Diana </dc:creator>
	<dc:subject xml:lang="en">ammonium sulphate fraction</dc:subject>
	<dc:subject xml:lang="en">BAPNA</dc:subject>
	<dc:subject xml:lang="en">viscera</dc:subject>
	<dc:subject xml:lang="en">little tuna</dc:subject>
	<dc:subject xml:lang="en">trypsin enzyme</dc:subject>
	<dc:subject xml:lang="id">BAPNA</dc:subject>
	<dc:subject xml:lang="id">enzim tripsin</dc:subject>
	<dc:subject xml:lang="id">fraksi amonium sulfat</dc:subject>
	<dc:subject xml:lang="id">ikan tongkol</dc:subject>
	<dc:subject xml:lang="id">jeroan</dc:subject>
	<dc:description xml:lang="id">Usus ikan tongkol merupakan bagian saluran pencernaan ikan yang memiliki pH neteral sehingga berpotensi sebagai sumber enzim, yaitu enzim tripsin. Enzim tripsin dari jeroan ikan bisa menjadi alternatif dari enzim tripsin komersil yang berasal dari babi dan sapi. Penelitian ini bertujuan menganalisis karakteristik fraksi amonium sulfat enzim tripsin dari usus ikan tongkol. Tahapan penelitian diawali dengan ekstraksi enzim tripsin dari usus ikan tongkol lalu difraksinasi menggunakan amonium sulfat (0-80%). Fraksi terbaik dikarakterisasi suhu, pH, pengaruh ion logam, stabilitas terhadap NaCl, dan substrat optimum serta dilakukan analisis kinetika reaksi. Pengukuran aktivitas enzim menggunakan substrat N-α-benzoyl-DL-arginine-p-nitroanilide (BAPNA). Hasil penelitian menunjukkan bahwa ekstrak kasar tripsin memiliki aktivitas sebesar 0,205 U/mL. Aktivitas enzim tripsin tertinggi terdapat pada fraksi amonium sulfat fraksi 40-50% sebesar 0,248 U/mL. Enzim bekerja optimum bekerja pada suhu 60°C dan pH 9. Ion logam ZnCl2 dan CaCl2 menghambat aktivitas tripsin, sedangkan MnCl2, CuCl2, dan NaCl dapat meningkatkan aktivitas tripsin. Aktivitas tripsin stabil pada NaCl 5-30%. Enzim tersebut memiliki nilai Vmaks sebesar 0,42 mmol/s dan nilai Nilai Km sebesar 1,12 mM</dc:description>
	<dc:description xml:lang="en">Intestine is part of the digestive tract of fish having neutral pH. Thus, fish intestine is a potential source of typsin and can be an alternative source to the commercial trypsin enzyme derived from pork and cattle. This study was aimed to analyze the characteristics of the ammonium sulphates fraction of the trypsin enzyme from tuna intestine. The research began with the extraction of the trypsin enzyme from the little tuna intestine and followed up by fractionation using ammonium sulphates (0-80%). Optimum temperature and pH as well as effects of metal ions, stability to NaCl, optimum substrate and reaction kinetics were determined. Enzyme activity was measured using N-α-benzoyl-DL-arginine-p-nitroanilide (BAPNA). The results showed that the trypsin crude extract had an activity of 0.205 U / mL. The highest enzyme activity was found in the ammonium sulphates fraction of 40-50% . The enzyme worked optimally at 60°C and pH 9. Metal ions including ZnCl2 and CaCl2 inhibited trypsin activity, while MnCl2, CuCl2, and NaCl increased trypsin activity. Trypsin activity was stable at 5-30% NaCl. The enzyme had a Vmax value of 0.42 mmol/s and a Km value of 1.12 mM.</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>2020-09-04</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>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://journal.ipb.ac.id/jphpi/article/view/32221</dc:identifier>
	<dc:identifier>10.17844/jphpi.v23i2.32221</dc:identifier>
	<dc:source xml:lang="id">Jurnal Pengolahan Hasil Perikanan Indonesia; Vol 23 No 2 (2020):  Jurnal Pengolahan Hasil Perikanan Indonesia 23(2); 372-382</dc:source>
	<dc:source xml:lang="en">Jurnal Pengolahan Hasil Perikanan Indonesia; Vol. 23 No. 2 (2020):  Jurnal Pengolahan Hasil Perikanan Indonesia 23(2); 372-382</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/32221/20386</dc:relation>
	<dc:rights xml:lang="en">Copyright (c) 2020 Tati Nurhayati, Roni Nugraha, Diana  Ningdya Lihuana</dc:rights>
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