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Digestive Enzyme Activities in Barred Loach (Nemacheilus fasciatus, Val., 1846.): Effect of pH and Temperature

Molekul: Jurnal Ilmiah Kimia · Vol. 17 No. 2 (2022) · hlm. 219–228

DOI
10.20884/1.jm.2022.17.2.5557
ISSN
2503-0310, 1907-9761
Terbit
2022-07-21
Penerbit
Universitas Jenderal Soedirman
Bahasa
eng

Abstrak

This study aims to determine the total protease, lipase, and amylase activities at different pHs, as well as pepsin and trypsin-like at different temperatures. A total of 240 individuals have been used in this study. Enzyme activity was measured by the spectrophotometer method. The effect of pH was evaluated on protease, lipase, and amylase activity, while the effect of temperature was evaluated on pepsin and trypsin-like activities.The results showed that the total protease activity at pH 7.0-10.0 was significantly higher than pH 1.7-5.0 (P <0.05). Furthermore, the activity of lipase was significantly higher at pH 5.0-7.0 than pH 1.7, 3.4, and 10.0. Also, the activity of amylase at pH 7.0-8.0 was significantly higher (p <0.05) than pH 1.7-5.0 and pH 10.0. Moreover, the pepsin-like activity in the anterior gut was significantly higher (p <0.05) than the posterior gut.Conversely, trypsin-like activity in the posterior gut was significantly higher (p <.05) than the anterior gut. Additionally, the pepsin-like activity was significantly higher at 45°C compared to different temperatures (p <0.05), whereas trypsin-like was significantly (p <0.05) higher at 60 °C than othertemperatures. Conclusively, the total protease and amylase activity was higher under neutral to slightly alkaline conditions, while lipase was higher under acidic to neutral conditions. Furthermore, the pepsin-like activity was only found in the anterior gut, whereas trypsin-like was higher in the posterior gut. The optimal temperature for pepsin-like and trypsin-like activity was 45 °C and 60 °C, respectively.

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  • Jenderal Soedirman University
  • National Research and Innovation Agency
  • Tsinghua University
  • University of Bahri
  • Southeast Asian Fisheries Development Center
  • Nasional University
  • IPB University
  • Afiliasi tidak diketahui
  • Organisasi berbeda
  • Organisasi sama
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Rekan penulisOrganisasiArtikel bersama
Atang AtangJenderal Soedirman University7
Hana HanaJenderal Soedirman University7
Yulia SistinaJenderal Soedirman University5
Phuping SucharitakulTsinghua University5
Eko SetiyonoJenderal Soedirman University5
Sorta Basar Ida SimanjuntakJenderal Soedirman University3
Hanan Hassan Alsheikh MahmoudUniversity of Bahri3
Joko PamungkasNational Research and Innovation Agency3
Mellya Rizki PitrianiJenderal Soedirman University3
I G A Ayu Ratna PuspitasariAfiliasi tidak diketahui2
Endah Sri PalupiJenderal Soedirman University2
Frolan A. AyaSoutheast Asian Fisheries Development Center2
Joko PamungkasNational Research and Innovation Agency2
Yuni ApriyantiNational Research and Innovation Agency2
Asrul Sahri SiregarJenderal Soedirman University1
Purnama SukardiJenderal Soedirman University1
Edy YuwonoNasional University1
Ridwan AffandiIPB University1
Havidh Ardika SyahputraJenderal Soedirman University1
Imelda ImeldaJenderal Soedirman University1
Siti WinasisJenderal Soedirman University1

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Sumber metadata: OAI-PMH (metadata jurnal) https://jos.unsoed.ac.id/index.php/jm/oai, pertama di-harvest 9 Nov 2026, terakhir terlihat 9 Nov 2026.
Metadata asli (oai_dc)
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	<dc:title xml:lang="en-US"> Digestive Enzyme Activities in Barred Loach (Nemacheilus fasciatus, Val., 1846.): Effect of pH and Temperature</dc:title>
	<dc:creator>Susilo, Untung</dc:creator>
	<dc:creator>Rachmawati, Farida Nur</dc:creator>
	<dc:creator>Wibowo, Eko Setio</dc:creator>
	<dc:creator>Pradhyaningrum, Ristiandani R.</dc:creator>
	<dc:creator>Okthalina, Koni</dc:creator>
	<dc:creator>Mulyani, Muthiara N. A.</dc:creator>
	<dc:description xml:lang="en-US">This study aims to determine the total protease, lipase, and amylase activities at different pHs, as well as pepsin and trypsin-like at different temperatures. A total of 240 individuals have been used in this study. Enzyme activity was measured by the spectrophotometer method. The effect of pH was evaluated on protease, lipase, and amylase activity, while the effect of temperature was evaluated on pepsin and trypsin-like activities.The results showed that the total protease activity at pH 7.0-10.0 was significantly higher than pH 1.7-5.0 (P &amp;lt;0.05). Furthermore, the activity of lipase was significantly higher at pH 5.0-7.0 than pH 1.7, 3.4, and 10.0. Also, the activity of amylase at pH 7.0-8.0 was significantly higher (p &amp;lt;0.05) than pH 1.7-5.0 and pH 10.0. Moreover, the pepsin-like activity in the anterior gut was significantly higher (p &amp;lt;0.05) than the posterior gut.Conversely, trypsin-like activity in the posterior gut was significantly higher (p &amp;lt;.05) than the anterior gut. Additionally, the pepsin-like activity was significantly higher at 45°C compared to different temperatures (p &amp;lt;0.05), whereas trypsin-like was significantly (p &amp;lt;0.05) higher at 60 °C than othertemperatures. Conclusively, the total protease and amylase activity was higher under neutral to slightly alkaline conditions, while lipase was higher under acidic to neutral conditions. Furthermore, the pepsin-like activity was only found in the anterior gut, whereas trypsin-like was higher in the posterior gut. The optimal temperature for pepsin-like and trypsin-like activity was 45 °C and 60 °C, respectively.</dc:description>
	<dc:publisher xml:lang="en-US">Universitas Jenderal Soedirman</dc:publisher>
	<dc:date>2022-07-21</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://jos.unsoed.ac.id/index.php/jm/article/view/5557</dc:identifier>
	<dc:identifier>10.20884/1.jm.2022.17.2.5557</dc:identifier>
	<dc:source xml:lang="en-US">Molekul; Vol 17 No 2 (2022); 219-228</dc:source>
	<dc:source>2503-0310</dc:source>
	<dc:source>1907-9761</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://jos.unsoed.ac.id/index.php/jm/article/view/5557/3187</dc:relation>
	<dc:rights xml:lang="en-US">Copyright (c) 2022 Molekul</dc:rights>
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