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Karakteristik Beberapa Jenis Antibiotik Berdasarkan Pola Difraksi Sinar-X (XRD) Dan Spektrum FTIR Mirzan T Razzak; Sandra Hermanto; Priyambodo Priyambodo
Jurnal Kimia Valensi Jurnal Valensi Volume 1, No.3, November 2008
Publisher : Syarif Hidayatullah State Islamic University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (219.768 KB) | DOI: 10.15408/jkv.v1i3.221

Abstract

Telah dilakukan pengukuran karakteristik difraksi sinar-x (XRD) terhadap beberapa jenisantibiotik. Penelitian ini bertujuan untuk memahami karakteristik difraksi sinar-x suatuantibiotik sebagai upaya untuk identifikasi antibiotik secara cepat. Dalam penelitian ini diamatikarakteristik difraksi sinar-x dari 15 (lima belas) antibiotik yang tersedia di pasaran. SpektrumXRD diukur pada sudut 2 antara 5 – 75 untuk dibandingkan dan dievaluasi mengenai bentukkristalnya. Selanjutnya diukur pula spektrum XRD dari pencampuran antibiotik dengan tepungtapioka. Pengukuran spektrum infrared dengan FTIR juga dilakukan untuk menguji konsistensihasil evaluasi spektrum XRD. Hasil penelitian menunjukkan bahwa amoxicillin dan ampicillinmempunyai struktur kristal yang sama, yaitu orthorombic primitif. Sayangnya baik XRDmaupun FTIR, tidak memberikan nilai kuantitatif pada antibiotik. Oleh sebab itu, perbedaankonsentrasi dengan pencampuran tepung tapioka tidak dapat dideteksi. Walaupun demikian,metode ini terbukti dapat digunakan untuk membedakan komposisi zat penyusun antibiotiksecara cepat dan akurat.
Spesifitas dan Sensitifitas Antibodi Anti eRF3 Ragi Saccharomyces cerevisia Sandra Hermanto
Jurnal Kimia Valensi Jurnal Valensi VOLUME 1, NO.1, NOVEMBER 2007
Publisher : Syarif Hidayatullah State Islamic University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (798.24 KB) | DOI: 10.15408/jkv.v1i1.211

Abstract

Protein eRF3 (eukaryotic release factor-3) merupakan salah satu protein yang berperan padaproses terminasi translasi. Protein ini bersama-sama dengan eRF1 (eukaryotic release factor-1) saling berinteraksi membentuk kompleks release factor dalam memediasi pelepasan rantaipolipeptida dari ribosom. Untuk memahami mekanisme terminasi translasi dalam sistemeukariot telah dilakukan studi struktur fungsi eRF1 yang dilanjutkan dengan studi interaksi invitro eRF1 mutan dan eRF1 wild type dengan eRF3. Namun demikian, hasil deteksi dari studiinteraksi in vitro sulit terdeteksi secara kuantitatif. Untuk dapat mengkuantisasi pita-pitaeRF3 hasil studi interaksi in vitro diperlukan antibodi anti eRF3. Konstruksi antibodi antieRF3 telah dilakukan, tetapi antibodi ini belum terkarakterisasi dengan baik. Tahapanselanjutnya dilakukan analisa Western blot dengan cara mengukur tingkat spesifitas dansensitifitas antibodi anti eRF3 terhadap protein eRF3. Spesifitas antibodi ditentukanberdasarkan kemampuan antibodi ini dalam mengenali epitop protein eRF3 dari berbagaiprotein yang terdapat pada crude extract ragi, sedangkan sensitifitasnya ditentukan melaluivariasi jumlah antigen (eRF3) yang berinteraksi dengan antibodi tersebut. Hasil analisaWestern blot menunjukkan spesifitas antibodi anti eRF3 masih relatif baik dimana antibodiini mampu mengenali epitop protein eRF3 yang ditandai dengan munculnya pita tunggal(76,6 kDa) setelah antibodi ini direaksikan dengan crude extract ragi yang mengandungprotein eRF3. Sensitifitas antibodi ini juga relatif tinggi, karena antibodi ini mampumendeteksi protein eRF3 hingga jumlah yang relatif rendah (0,77 ng). Namun demikianantibodi ini belum cukup mampu mendeteksi protein eRF3 yang secara alamiah terdapat padacrude extract ragi. Hal ini kemungkinan besar disebabkan karena level ekspresi eRF3 dalamsel ragi yang relatif rendah jika dibandingkan dengan protein ribosom.
Perbedaan Profil Protein Produk Olahan (Sosis) Daging Babi dan Sapi Hasil Analisa SDS-PAGE Sandra Hermanto; Cut Dhien K Meutia
Jurnal Kimia Valensi Jurnal Valensi Volume 1, No.4, Mei 2009
Publisher : Syarif Hidayatullah State Islamic University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (416.222 KB) | DOI: 10.15408/jkv.v1i4.247

Abstract

Meningkatnya kebutuhan konsumsi protein hewani, khususnya daging tidak luput dari beragammasalah, di antaranya kekhawatiran adanya kandungan babi sebagai bahan baku dalam produk olahan(sosis). Tujuan dari penelitian ini adalah untuk mengetahui profil protein daging sapi dan babi dalamkeadaan mentah dan produk olahan (sosis) berdasarkan karakteristik berat molekul (BM) sebagai dasaruntuk pengembangan metode analisa kehalalan pangan. Penelitian diawali dengan isolasi protein daridaging mentah (sapi dan babi) dan sosis (sapi dan babi) yang meliputi sosis komersil dan olahansendiri. Isolat protein yang dihasilkan dari masing-masing sampel dikarakterisasi dengan SodiumDodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE) 10%(v/v) untuk mengetahui BM(kDa) protein terlarut. Penghitungan BM dilakukan melalui regresi linear y =-0,9259x+2,2188 denganR2=0,9662, yang diperoleh dari protein standar sebagai marker. Hasil penelitian yang dilakukanmenunjukkan terdapat 3 pita spesifik pada sapi mentah yang tidak dimiliki babi mentah yaitu pada Rf0,29; 0,71; dan 0,88 dengan BM sekitar 89,2 kDa; 36,4 kDa dan 25,3 kDa. Selain itu pada sosis sapikomersil ditemukan pita tebal dengan BM sekitar 45,1 kDa dan pada sosis babi komersil ditemukanpita tebal dengan BM sekitar 69 kDa. Secara keseluruhan, pada sampel sosis, protein yang terkandungsulit untuk dikarakterisai dengan elektroforesis SDS-PAGE karena sebagian protein tersebut telahterdegradasi.
Aktivitas Senyawa Antidiabetes Ektrak Etil Asetat Daun Pandan Wangi (Pandanus Amaryllifolius Roxb.) Dede Sukandar; Sandra Hermanto; Imamah Al Mabrur
Jurnal Kimia Valensi Jurnal Valensi Volume 1, No.6, Mei 2010
Publisher : Syarif Hidayatullah State Islamic University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (544.838 KB) | DOI: 10.15408/jkv.v1i6.238

Abstract

Penelitian ini dilakukan untuk mengetahui aktivitas antidiabetes dari ekstrak etil asetat daun pandanwangi (Pandanus amaryllifolius Roxb.) menggunakan metode α-glukosidase. Ekstrak dibuat dengancara perendaman menggunakan etil asetat. Uji antidiabetes dilakukan dengan menggunakan enzim α-glukosidase. Ekstrak etil asetat daun pandan wangi bersifat antidiabetes dengan aktivitaspenghambatan (IC50) sebesar 94,23 ppm. Hasil analisa GCMS menunjukkan ekstrak etil asetat daunpandan wangi mengandung senyawa aktif asam lemak dan turunannya, terpenoid, dan steroid.
Uji Toksisitas Ekstrak Daun Pandan Wangi (Pandanus amaryllifolius Roxb.) Dengan Metode Brine Shrimp Lethality Test (BSLT) Dede Sukandar; Sandra Hermanto; Emi Lestari
Jurnal Kimia Valensi Jurnal valensi Volume 1, No.2, Mei 2008
Publisher : Syarif Hidayatullah State Islamic University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1101.673 KB) | DOI: 10.15408/jkv.v1i2.217

Abstract

Telah dilakukan penelitian untuk mengetahui toksisitas dari ekstrak daun pandan wangimenggunakan metode Brine Shrimp Lethality Test (BSLT). Ekstrak dibuat dengan cara maserasimenggunakan tiga macam pelarut, yaitu butanol, etil asetat, dan petroleum eter. Uji toksisitasdilakukan dengan menggunakan larva udang Artemia salina Leach yang berumur 48 jam. Efektoksik masing-masing ekstrak diidentifikasi dengan presentase kematian larva udangmenggunakan analisis probit (LC50). Ekstrak aktif kemudian diuji kandungan fitokimianya dansenyawa bioaktif yang terkandung di dalamnya dengan menggunakan GC-MS. Hasilnyamenunjukkan ekstrak etil asetat bersifat toksik (LC50 : 288,4 ppm). Senyawa yang terkandungdalam ekstrak etil asetat adalah senyawa terpenoid dan steroid.
The HMG-CoA Reductase Inhibitor Activities of Soy Protein Hydrolysates from Papain Hydrolysis Sandra Hermanto; Aldi Octavio; Azrifitria Azrifitria; Susi Kusumaningrum
Molekul Vol 16, No 2 (2021)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (334.752 KB) | DOI: 10.20884/1.jm.2021.16.2.724

Abstract

The search for an HMG-CoA reductase inhibitor agent as a safe and inexpensive alternative treatment for hypercholesterolemia has been carried out using soy protein hydrolysates as one of the bioactive peptide sources. This study was conducted to explore the potency of soy protein hydrolysates as an anti hypercholesterolemia agent by an in vitro assay, through the inhibition capacity of the HMG-CoA (3-hydroxy-3-methyl glutaryl-coenzyme A) reductase enzyme as a key component of cholesterol biosynthesis. Sample preparation started with soy protein isolation through acid precipitation and separated by centrifugation. The samples were analyzed the proximate content and hydrolyzed by papain enzyme at concentration 0.2% (w/v), for 0-6 hours and at 37, 50, and 55 oC. The protein hydrolysates were subsequently evaluated for hydrolysis degree (% DH), hydrolysates profile with SDS-PAGE (Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis), and anti-cholesterol assay through HMG-CoA reductase inhibition tests. The sample with the highest inhibition activity was fractionated using gel filtration chromatography (Sephadex G-10) and the molecular weight of fractions was characterized by LCMS QTOF (Liquid Chromatography-Mass Spectrometry Quadrupole Time-of-Flight) for molecular weight determination. The results indicated the optimum hydrolysis conditions of soy protein isolates were obtained at 3 hours incubation, at 50 °C with DH 33.39% and the inhibition value was 95.65% (protein concentration 39.21 μg / mL). LCMS data showed the molecular weight of fractionated peptides were 1514 and 2029 Da. We assumed that both peptides have the same affinity as previous peptides in inhibiting HMG-CoA reductase.
Identification of Differentially Expressed Protein from Electrical Stunning of Broiler Chickens Meat Protein Sandra Hermanto; Maya Ina Sholaikah; Sri Suci Mulyani
Molekul Vol 11, No 1 (2016)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (463.618 KB) | DOI: 10.20884/1.jm.2016.11.1.196

Abstract

Identification of differentially expressed protein from the muscle tissue of broiler chicken meat with different conditions of pre-slaughter has been done. Each sample (6 broilers aged 21 days, 1 kg of weight ) was prepared through the process of pre-slaughter with 3 conditions, the first sample slaughtered in a conventional way which untreated electrical stunning, while the second and third sample of the chicken was prepared by using electrical stunning with 1 A and 25 Volts for 5 seconds and 1 A, 125 Volts for 30 seconds. Two biological replicate were done for each of samples. Muscle tissue protein extracted in Tris HCl pH 8.0 and the proteins separation by using SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis). Identification of differentially expressed protein performed by densitometry to identify the profile of the resulting proteins. The results of this study showed that the protein bands constructed in the range of 8.5-140 kDa and 9 dominant protein bands with different relative intensities. Densitogram analysis results showed there are two specific protein bands appear on the results of the electrical stunning which more extensive over expression. This indicates the electrical stunning of slaughter process may triggered the expression levels of certain proteins that do not occur in the nonelectrical stunning.
AKTIVITAS ANTIBAKTERI EKSTRAK BIJI KAPULAGA (Amomum compactum Sol. Ex Maton) Dede Sukandar; Sandra Hermanto; Eka Rizki Amelia; Muhamad Zaenudin
Jurnal Kimia Terapan Indonesia Vol 17, No 2 (2015)
Publisher : Research Center for Chemistry - LIPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (648.526 KB) | DOI: 10.14203/jkti.v17i2.28

Abstract

Testing of antibacterial activity against ethyl acetate extract local cardamom seeds (Amomum compactum Sol. Ex Maton) has been performed. Extraction was carried out using the soxhlet method with methanol solvent and liquid-liquid partitioned with n-hexane, ethyl acetate and n-butanol solvent, antibacterial activity test was performed using the disc diffusion method, fractionation using column chromatography and characterization of active fractions using chromatography GCMS, UV-vis and FTIR spectroscopy. The test results showed that the antibacterial activity of ethyl acetate extract had the highest antibacterial activity against S. aureus and E. coli with inhibition zone diameter of respectively 15.15 ± 1.34 and 13.50 ± 0.70 mm at a concentration of 3200 mg/mL. Results of fractionation of the ethyl acetate fraction using column chromatography with a mobile phase of ethyl acetate: n-hexane (3: 2) yielded three fractions, namely F1 (14.6 mg), F2 (8.1 mg) and F3 (4.6 mg). Fraction 2 had the highest antibacterial activity against S. aureus with inhibition zone diameter of 12.34 ± 0.07 mm at a concentration of 800 ug/mL. The results of the characterization of the fraction 2 obtained using GCMS analysis of three antibacterial compounds suspected of 2.9-dihydroxy-1,8-cineol; 2,4-dihydroxy-1,8-cineol and 2,2-methylene bis [6- (1,1-dimethylethyl) -4-ethyl] phenol. The results of the F2 fraction characterization using UV-Vis spectroscopy showed the presence of group C = C conjugated chromophore at λmax 223 nm and are based on analysis using FTIR there -OH alcohol functional group (3372 cm-1), aliphatic -CH (2926 and 2854 cm-1) , C = C (1695 cm-1), aliphatic CH2 (1402 cm-1), CH3 aliphatic (1384 cm-1), and C-O (1203; 1126; 1091 and 1043 cm-1). Keywords: Antibacterial, S. aureus, E. coli, Amomum compactum Sol. Ex Maton, disk diffusion
SIFAT FISIKO KIMIA DAN AKTIVITAS ANTIOKSIDAN MINYAK KELAPA MURNI (VCO) HASIL FERMENTASI RHIZOPUS ORIZAE Dede Sukandar; Sandra Hermanto; Eva Silvia
Jurnal Kimia Terapan Indonesia Vol 11, No 2 (2009)
Publisher : Research Center for Chemistry - LIPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (5284.225 KB) | DOI: 10.14203/jkti.v11i2.157

Abstract

Research on physicochemical properties and antioxidant activity of VCO obtained from Rhizopus orizaefermentation had been done. Antioxidant activity was determined by DPPH method. Production of VCO had been carried out from coconut sample obtained from Pandeglang region with fermentation by Rhizopusorizae in variation of inoculum asfollow 2%, 5%, 7%, 10% and 12 %. Physicochemical test consist of density, refractive index, water content, free fatty acid, iodine value, peroxide value while the composition of fatty acid determined by GCMS, The result showed that variation of inoculum had significantly 0,024 influenced the yielded of VCO producted. Based on this result, quality of VCO still in the range of CODEX Standard, 19-1991rev.2-1999. It was found that antioxidant activity of VCO only 6.3% at 1000 ppm. The composition offatty acid based in lauric acid content measured by GCMS showed a significant result (49.48%-50%) agreed with COD EX Standard.Keyword: Antioxidant, DPPH, veo, Fermentation,Rhizopus oriza.
AKTIVITAS ANTIDIABETES EKTRAK ETIL ASETAT DAUN PANDAN WANGI (Pandanus amaryllifolius Roxb.) Dede Sukandar; Sandra Hermanto; Imamah Al Mabrur
Jurnal Kimia Terapan Indonesia Vol 12, No 2 (2010)
Publisher : Research Center for Chemistry - LIPI

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (2853.89 KB) | DOI: 10.14203/jkti.v12i2.215

Abstract

This research done to know activity antidiabetes from fragrant screw pine leaf ethyl acetate extract (Pandanus amaryllifolius Roxb.) applies method aglukosidase. Extract is made by the way ofmaceration to apply ethyl acetate. Test antidiabetes is done by using enzyme a-glukosidase and PNP-a-D-glukopiranosida. Fragrant screw pine leaf ethyl acetate extract haves the character of antidiabetes with resistance activity, IC50 value as 94,23 ppm. Result of GCMS identification shows fragrant screw pine leaf ethyl acetate extract contains active compound of its the fatty acid and deriuaies, terpenoids, and steroid.Keyword : Antidiabetes, Ekstrak Etil Asetat, Pandanus amaryllifolius Roxb, a-glukosidase, PNP-a-D-glukopiranosida.