Purifikasi parsial dan karakterisasi enzim katepsin dari ikan cakalang (Katsuwonus pelamis) Partial purification and characterization of cathepsins from skipjack tuna (<i>Katsuwonus pelamis</i>)
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ammonium sulfate, autolysis, enzyme activity, enzyme kinetics, protease
Abstract
Cathepsin enzymes are crucial in the post-harvest protein degradation of fish, impacting the quality stability of skipjack tuna (Katsuwonus pelamis) meat, a valuable fishery commodity. This study aimed to partially purify and characterize the cathepsin enzyme from skipjack tuna meat. Post-rigor skipjack tuna cathepsin was extracted, subjected to ammonium sulfate precipitation (0-80% saturation), and analyzed for enzyme activity, protein concentration, optimum pH (3-7), optimum temperature (20-60°C), and enzyme kinetics using hemoglobin as a substrate. The results revealed a specific activity of 0.67±0.11 U/mg in the crude extract, which increased to 7.50 U/mg at the 60-70% precipitation fraction (purification fold of 11.28 times and yield of 12.98%). The skipjack tuna cathepsin exhibited optimum pH and temperature of 4 (activity 0.55 U/mg) and 40°C (0.70 U/mg), respectively, with kinetic parameters of km 4.09% and Vmax 1.59 U/mL. This confirms the sensitivity of acid proteases to environmental conditions. These findings provide a foundation for controlling autolysis to extend the shelf-life of skipjack tuna.
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References
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Copyright (c) 2026 Riki Kurniawan, Evira Lisnaina, Alfahreyzha Agung Prasetya, Adz Dzariyaat Khair, Maria Dolorosa Sare, Dimas Anugrah, Nurlita Tadzlila Wijayanti, Tati Nurhayati
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