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dc.contributor.advisorNurhayati, Tati
dc.contributor.advisorAbdullah, Asadatun
dc.contributor.authorAuliya, Fakhrina
dc.date.accessioned2023-08-07T02:37:47Z
dc.date.available2023-08-07T02:37:47Z
dc.date.issued2023-08
dc.identifier.urihttp://repository.ipb.ac.id/handle/123456789/123137
dc.description.abstractKebutuhan enzim di Indonesia sangat tinggi dan masih diimpor dari negara lain. Tripsin komersial biasanya diekstraksi dari pankreas babi dan sapi, sehingga diperlukan sumber alternatif lainnya yang bersumber dari ikan, yaitu usus, hati, dan limpa ikan tuna. Penelitian ini bertujuan menentukan karakteristik dan stabilitas enzim tripsin dalam NaCl, serta hubungan usus, hati, dan limpa ikan tuna terhadap aktivitas tripsin menggunakan Principal Component Analysis (PCA). Aktivitas tripsin berada pada kondisi optimum pada suhu 60 ̊C dan pH 8 dengan nilai aktivitas spesifik pada usus sebesar 0,948±0,114 U/mg; hati sebesar 0,610±0,029 U/mg; dan limpa sebesar 0,605±0,159 U/mg. Kecepatan reaksi maksimum (Vmaks) menunjukkan nilai usus yang paling besar sebesar 0,248 mmol/s, diikuti oleh hati 0,138 mmol/s, dan limpa 0,096 mmol/s, sedangkan nilai konstanta (Km) yang diperoleh usus sebesar 2,342 mM; hati sebesar 2,268 mM, dan limpa sebesar 1,276 mM. Bobot molekul pada tripsin berkisar antara 20-30 kDa. Konsentrasi NaCl yang tinggi akan menyebabkan aktivitas semakin menurun. Bagian usus, hati, dan limpa memiliki korelasi positif.id
dc.description.abstractThe need for enzymes in Indonesia is very high and they are still imported from other countries. Commercial trypsin is usually extracted from the pancreas of pigs and cattle, so that other alternative sources are needed from fish, namely the intestines, liver and spleen of tuna. The relationship between intestine, liver and spleen of tuna trypsin activity using Principal Component Analysys (PCA) was used to determine characterisics and stability of the trypsin enzyme in NaCl as the study aims. Trypsin activity was at its optimum at a temperature of 60 ̊C and pH 8 with a specific activity value in the intestine of 0,948 ± 0,114 U/mg; liver of 0,610 ± 0,029 U/mg; and spleen of 0,605 ± 0,159 U/mg. The maximum reaction speed (Vmax) showed the largest intestinal value of 0,248 mmol/s, followed by the liver 0,138 mmol/s, and the spleen 0,096 mmol/s, while the constant value (Km) obtained by the intestine was 2,342 mM; liver of 2,268 mM, and spleen of 1,276 mM. The molecular weight of trypsin ranges from 20-30 kDa. The high concentration of NaCl decreased the activity. Sections of intestine, liver, and spleen had a positive correlation.id
dc.language.isoidid
dc.publisherIPB Universityid
dc.titleKarakteristik dan Stabilitas Enzim Tripsin dalam NaCl yang diisolasi dari Usus, Hati, dan Limpa Ikan Tunaid
dc.title.alternativeCharacteristics and Stability of Trypsin Enzyme in NaCl Isolated from Intestine, Liver, and Spleen of Tunaid
dc.typeUndergraduate Thesisid
dc.subject.keywordkarakteristik enzim tripsinid
dc.subject.keywordstabilitas NaClid
dc.subject.keywordjeroan tunaid


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