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Optimasi Produksi Enzim Amilase dari Bakteri Laut Jakarta (Arthrobacter arilaitensis)   Purnawan, A.; Capriyanti, Y.; Kurniatin, PA.; Rahmani, N.; ., Yopi
JURNAL BIOLOGI INDONESIA Vol 11, No 2 (2015): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/jbi.v11i2.2195

Abstract

ABSTRACTAmylase is one of the most important industrial enzymes which can be used in a number of industrial processes including food industry, textile, paper industry, renewable energy, and pharmaceutical. This study reports the environmental conditions and nutrient media for amylase production from marine bacterium Arthrobacter arilaitensis. Various parameters such as substrate concentration, pH medium, temperature of fermentation, co-substrate, and nitrogen source was determined to obtain the optimum conditions. Maximum amylase enzyme production was obtained at starch concentration 1%, pH 7, temperature fermentation 30°C, co-substrate maltose with activity 2.7 U/mL. While the addition of several nitrogen sources was given decreased amylase activity, such as addition casein was decreased the activity into 2.3 U/mL. Keywords: Arthrobacter arilaitensis, amylase activity, optimization, co-substrate, pH, temperature, substrate, nitrogen source 
Stabilitas Laju Fotosintesis dan Produktivitas Rimpang Genotipe Curcuma aeruginosa dan Curcuma zanthorrhiza Djarot Sasongko Hami Seno; Mohamad Rafi; Maria Bintang; Popy Asri Kurniatin; Waras Nurcholis
Jurnal Agronomi Indonesia (Indonesian Journal of Agronomy) Vol. 48 No. 1 (2020): Jurnal Agronomi Indonesia
Publisher : Indonesia Society of Agronomy (PERAGI) and Department of Agronomy and Horticulture, Faculty of Agriculture, IPB University, Bogor, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (567.533 KB) | DOI: 10.24831/jai.v48i1.30100

Abstract

Rimpang temu hitam (Curcuma aeruginosa Roxb.) merupakan bahan baku herbal penting yang berkhasiat sebagai antimikroba, antikanker, dan antioksidan. Dengan demikian, penting untuk mendapatkan tanaman temu hitam yang memiliki produktivitas rimpang dengan stabilitas yang luas pada kondisi lingkungan yang beragam. Penelitian ini bertujuan untuk mengevaluasi interaksi genotipe x lingkungan menggunakan analisis additive main effects and multiple interaction (AMMI) terhadap karakter laju fotosintesis dan produktivitas rimpang genotipe temu hitam. Dua puluh genotipe temu hitam dan tiga varietas temulawak (C. zanthorrhiza Roxb.) dievaluasi di tiga lokasi percobaan (Bogor, Cianjur, dan Sukabumi) menggunakan rancangan acak kelompok lengkap teracak dengan pengulangan tiga kali. Interaksi genotipe x lingkungan memberikan pengaruh yang sangat nyata (p < 0.01) terhadap laju fotosintesis dan produktivitas rimpang. AMMI2 dapat menjelaskan 100% keragaman terhadap karakter laju fotosintesis dan produktivitas rimpang. G2, G10, G12, G13, G14, G16, G17, G19, dan G20 merupakan genotipe yang stabil pada produktivitas rimpang berdasarkan analisis AMMI. Karakter laju fotosintesis yang stabil ditemukan pada genotipe G4, G5, G6, G8, G11, G13, dan G14. Kata kunci: AMMI, genotipe, temu hitam, uji multilokasi, varietas
OPTIMASI PRODUKSI ENZIM AMILASE DARI BAKTERI LAUT JAKARTA (ARTHROBACTER ARILAITENSIS)   Purnawan, A.; Capriyanti, Y.; Kurniatin, PA.; Rahmani, N.; ., Yopi
JURNAL BIOLOGI INDONESIA Vol 11, No 2 (2015): JURNAL BIOLOGI INDONESIA
Publisher : Perhimpunan Biologi Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/jbi.v11i2.2195

Abstract

ABSTRACTAmylase is one of the most important industrial enzymes which can be used in a number of industrial processes including food industry, textile, paper industry, renewable energy, and pharmaceutical. This study reports the environmental conditions and nutrient media for amylase production from marine bacterium Arthrobacter arilaitensis. Various parameters such as substrate concentration, pH medium, temperature of fermentation, co-substrate, and nitrogen source was determined to obtain the optimum conditions. Maximum amylase enzyme production was obtained at starch concentration 1%, pH 7, temperature fermentation 30°C, co-substrate maltose with activity 2.7 U/mL. While the addition of several nitrogen sources was given decreased amylase activity, such as addition casein was decreased the activity into 2.3 U/mL. Keywords: Arthrobacter arilaitensis, amylase activity, optimization, co-substrate, pH, temperature, substrate, nitrogen source 
Penapisan Senyawa Polifenol sebagai Inhibitor Betalaktamase dengan Penambatan Molekuler POPI ASRI KURNIATIN; AKIMDO RULI SIMANJUNTAK; UKHRADIYA MAGHARANIQ SAFIRA PURWANTO
Gunung Djati Conference Series Vol. 34 (2023): Prosiding Seminar Nasional Kimia Tahun 2023
Publisher : UIN Sunan Gunung Djati Bandung

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

Betalaktamase adalah enzim yang mengkatalisis hidrolisis antibiotik Betalaktam sehingga dapat menyebabkan resistensi antibiotik. Bakteri yang dilaporkan dapat menghasilkan enzim Betalaktamase antara lain Klebsiella pneumoniae, Escherichia coli, Enterobacter sp., Salmonella sp., Proteus sp., Serratia marcescens, Shigella dysenteriae, Pseudomonas aeruginosa, dan Burkholderia cepacia. Saat ini resistensi terhadap antibiotik golongan Betalaktam semakin meluas. Penggunaan antibiotik ini seringkali dikombinasikan dengan inhibitor Betalaktamase seperti asam klavulanat, sulbaktam, dan tazobaktam untuk meningkatkan efisiensi terapi. Antibiotik betalaktam adalah antibiotik spektrum luas yang banyak menjadi pilihan untuk terapi. Oleh karena itu, pencarian kandidat inhibitor Betalaktamase untuk mencegah resistensi perlu dilakukan. Pada penelitian ini dilakukan penapisan senyawa polifenol sebagai inhibitor enzim Betalaktamase dengan metode penambatan molekuler. enapisan terhadap 112 senyawa polifenol dari database menghasilkan 27 senyawa yang memiliki energi bebas ikatan yang lebih baik dari ligan alami. Prediksi drug-likeness berdasarkan aturan Lipinski terhadap 27 senyawa tersebut menghasilkan 6 senyawa yang berpotensi, yaitu trans-resveratrol 3-O-glucuronide, apigenin-7-O-glucoside, cis-resveratrol 4'-sulfate, sulfuretin, dan apigenin. Berdasarkan visualisasi interaksi ligan-reseptor, keenam senyawa tersebut berinteraksi dengan residu katalitik enzim betalaktamase. Energi bebas ikatan terbaik ditunjukkan oleh trans-resveratrol 3-O-glucuronide sebesar -8,1 kkal/mol dan prediksi Ki sebesar 1,137 MikroM. Berdasarkan studi penambatan molekuler dan prediksi drug-likeness, 6 senyawa polifenol yang berpotensi tersebut dapat dilanjutkan untuk penelitian lebih lanjut.
In silico phylogenetic, physicochemical, and structural characteristics of phytase enzyme from ten Aspergillus species Ridwan Putra Firmansyah; Shobiroh Nuur Alimah; I Made Artika; Popi Asri Kurniatin
Menara Perkebunan Vol. 92 No. 1 (2024): 92(1), 2024
Publisher : INDONESIAN OIL PALM RESEARCH INSTITUTE

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22302/iribb.jur.mp.v92i1.559

Abstract

Phytic acid is a chemical compound consisting of inositol and phosphoric acid and is an antinutrient compound found in monogastric poultry feed ingredients made from cereal crops. Phytase hydrolyzes phosphoester bonds in phytic acid, releasing inorganic phosphate and phosphate esters. Aspergillus is a genus of molds that produce phytase and has been widely used in phytase production because they are easy to culture. This study aims to compare the structures, physicochemical characteristics, and phylogenetic relationships of phytases from several species of Aspergillus in silico as an initial screening step in obtaining the most suitable phytase to be used in poultry feed. Phylogenetic trees were constructed using MEGA 11 and physicochemical characteristics were analyzed using ProtParam. Protein structures were modeled with AlphaFold. The phytase structures were then docked with phytic acid using the YASARA Structure. The results showed that phytase 1QFX from Aspergillus niger, P34755 from A. awamori, and D5HQ11 from A. ficuum have very high similarity in terms of phylogenetics, sequences, physicochemical characteristics, and protein structures. The docking results from the three phytase structures showed that phytase 1QFX has the most negative ΔG value and the lowest Kd, which indicated the highest affinity to the phytic acid substrate. This research concludes that among the three phytase structures that have been compared and docked with phytic acid, phytase 1QFX from A. niger is the most suitable to be applied to poultry feed.