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All Journal Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam
Titania T. Nugroho
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Mathematics

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PEMEKATAN ENZIM SELULASE Penicillium sp. LBKURCC20 DENGAN PENGENDAPAN AMONIUM SULFAT 80% JENUH Masdalena Sinaga; Titania T. Nugroho; Andi Dahliaty
Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Vol 1, No 2 (2014): Wisuda Oktober 2014
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

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Abstract

Cellulase enzyme activity of Penicillium sp. LBKURCC20 Isolate of Riau can beincreased by concentrating the enzyme using 80% saturated solid ammonium sulfate(NH 4 ) 2 SO 4 anhydrous. Precipitated enzyme was redissolved by the addition of acetatebuffer solution pH 5.5 to 1/70 times its original volume. Cellulase enzyme activity wasdetermined using substrates CMC and avicel. CMCase and avicelase enzyme activity ofthe crude enzyme was (0.0164 ± 0.0036) U/mL and (0.003 ± 0.0025) U/mL,respectively. CMCase and avicelase enzyme activity after concentration was (0.219 ±0.0579) U/mL and (0.03 ± 0.03) U/mL, respectively. The test results showed that theactivity of concentrated CMCase increased 13.5 times and avicelase enzyme activityincreased 10 times after concentrating.
ISOLASI DAN PEMEKATAN ENZIM SELULASE Trichoderma sp. LBKURCC28 MENGGUNAKAN METODE PENGGARAMAN (NH 4 ) 2SO 4 80% SERTA PENENTUAN AKTIVITAS DAN AKTIVITAS SPESIFIK ENZIM Febry Kurniawan; Titania T. Nugroho; Andi Dahliaty
Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam Vol 1, No 2 (2014): Wisuda Oktober 2014
Publisher : Jurnal Online Mahasiswa (JOM) Bidang Matematika dan Ilmu Pengetahuan Alam

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Abstract

Cellulase enzyme activity can be increased by concentrating the enzyme using saturated ammonium sulfate ((NH4) 2SO4) 80%. Precipitated enzyme was redissolved by the addition of acetate buffer solution pH 5.5 to 1/70 times its original volume. Cellulase enzyme activity was determined using substrates CMC and avicel. The test results showed that the activity of concentrated CMCase increased 75 times and avicelase enzyme activity increased 9 times. Activity and specific activity concentrated CMCasewas 0,4060±0,0845 U/ml and 0,7306±0,1526 U/mg respectively, while activity and specific activity of concentrated avicelase were 0,0129±0,0182 U/ml and 0,0232±0,0328 U/mg respectively.
Co-Authors Andi Dahliaty Febry Kurniawan Masdalena Sinaga