Journals / Turkish Journal of Fisheries and Aquatic Sciences / 2026 / Cilt: 12 Sayı: 2

Purification and Characterization of Lipase from the Liver of Carp, Cyprinus carpio L. (1758), Living in Lake Tödürge (Sivas, TÜRKİYE)

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Publication Date
2012-04-01
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⚡ TL;DR(Too Long; Didn't Read)

It was observed that surface active agents, such as sodium dodecyl sulfate (SDS), Triton X-100 and Nataurocholate act as inhibitor on lipase activity.

📌 3 Key Takeaways

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Objective & Hypothesis:In this study, a lipase from the liver of Cyprinus carpio Linnaeus (1758) living in Tödürge Lake (Sivas) was purified with purification parameters of 90.38 μmol/dk.mg protein specific activity and 75.50 fold purity.
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Key Findings & Data:The purification procedure consisted of preparation of homogenate, precipitation with polyethylene glycol-6000 (PEG-6000) and chromatographic techniques including in Q sepharose, sephacryl S 200 HR and phenyl sepharose CL-4B, respectively.
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Conclusion & Impact:It was observed that surface active agents, such as sodium dodecyl sulfate (SDS), Triton X-100 and Nataurocholate act as inhibitor on lipase activity.
🔬Design:Makale
📍Scope:Comprehensive Sample
⚙️Variables:Cyprinus carpio · lipase activity · Q sepharose

Abstract

In this study, a lipase from the liver of Cyprinus carpio Linnaeus (1758) living in Tödürge Lake (Sivas) was purified with purification parameters of 90.38 μmol/dk.mg protein specific activity and 75.50 fold purity. The purification procedure consisted of preparation of homogenate, precipitation with polyethylene glycol-6000 (PEG-6000) and chromatographic techniques including in Q sepharose, sephacryl S 200 HR and phenyl sepharose CL-4B, respectively. The purified lipase showed a single band with approximately a molecular weight of 74 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). pH and temperature optimums for the purified enzyme were determined as 8.0 and 37 °C using p-nitrophenyl butirate (p-NPB) as substrate. Km and Vmax values were found as 0.17 mM p-NPB and 2.6 μmol/mL.dk, respectively. It was observed that surface active agents, such as sodium dodecyl sulfate (SDS), Triton X-100 and Nataurocholate act as inhibitor on lipase activity.

Özet

In this study, a lipase from the liver of Cyprinus carpio Linnaeus (1758) living in Tödürge Lake (Sivas) was purified with purification parameters of 90.38 μmol/dk.mg protein specific activity and 75.50 fold purity. The purification procedure consisted of preparation of homogenate, precipitation with polyethylene glycol-6000 (PEG-6000) and chromatographic techniques including in Q sepharose, sephacryl S 200 HR and phenyl sepharose CL-4B, respectively. The purified lipase showed a single band with approximately a molecular weight of 74 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). pH and temperature optimums for the purified enzyme were determined as 8.0 and 37 °C using p-nitrophenyl butirate (p-NPB) as substrate. Km and Vmax values were found as 0.17 mM p-NPB and 2.6 μmol/mL.dk, respectively. It was observed that surface active agents, such as sodium dodecyl sulfate (SDS), Triton X-100 and Nataurocholate act as inhibitor on lipase activity.

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Cite This Article

Görgün, S., Akpınar, M. A. (2012). Purification and Characterization of Lipase from the Liver of Carp, Cyprinus carpio L. (1758), Living in Lake Tödürge (Sivas, TÜRKİYE). Turkish Journal of Fisheries and Aquatic Sciences, Cilt: 12 Sayı: 2. https://ajindex.com/articles/1325146

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