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All Journal HAYATI Journal of Biosciences Jurnal Pengolahan Hasil Perikanan Indonesia ILMU KELAUTAN: Indonesian Journal of Marine Sciences Indonesian Journal of Cancer Chemoprevention BERITA BIOLOGI JURNAL BIOLOGI INDONESIA ANNALES BOGORIENSES Annales Bogorienses
Apon Zaenal Mustopa
Research Center for Biotechnology, Indonesian Institute of Sciences Jalan Raya Bogor km 46, Cibinong 16911, Bogor, Indonesia
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Earth & Planetary Sciences Immunology & microbiology Medicine & Pharmacology

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Journal : ANNALES BOGORIENSES

 1 
Enterococcus faecium 1.15 Isolated from Bakasam Showed Milk Clotting Activity Putranto, Wendry Setiyadi; Suradi, Kusmajadi; Chairunnisa, Hartati; Mustopa, Apon Zaenal; Giriwono, Puspo Edi; Kusumaningrum, Harsi Dewantari; Suhartono, Maggy Thenawidjaja
ANNALES BOGORIENSES Vol 21, No 1 (2017): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (499.913 KB) | DOI: 10.14203/ab.v21i1.293

Abstract

The Lactic Acid Bacteria with Milk Clotting Activity (MCA) were isolated from Bakasam, an Indonesian traditional fermented meat. The isolate screening was carried out using modified method of Skim Milk Agar and Milk Clotting Activity Test, and the isolate was then identified using 16S rRNA. We found 4 isolates that showed MCA of 18-20 SU/ml. Identification using 16S rRNA indicated that the isolate ALG.1.15 was 99% (FR3-F primer) and 99% (FR3-R primer) identic with Enterococcus faecium. The isolate potentially produced renin-like protease to subtitute renin from veal.  
Molecular Identification of Microalgae BTM 11 and its Lectin Isolation, Characterization, and Inhibition Activity Mustopa, Apon Zaenal; Isworo, Rhestu; Nurilmala, Mala; Susilaningsih, Dwi
ANNALES BOGORIENSES Vol 20, No 2 (2016): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ab.v20i2.251

Abstract

BTM 11 is unknown species of microalgae, but has active compounds that can inhibit viruses. One of proteins produced by microalgae is a lectin. Lectin is a carbohydrate-binding protein found in various microalgae that show antiviral and antibacterial activity. The purpose of this study was to perform identification of the species of microalgae BTM 11, isolation, characterization, and assay of lectin inhibitory activity. Microalgae BTM 11 was identified to have homology with Cyanobacterium 99% and Geitlerinema sp 98%. Lectin of microalgae BTM 11 was isolated by ammonium sulfate precipitation of 75% with a molecular weight of 17 kDa. Lectin protein activity of microalgae BTM 11 was able to inhibit the enzyme activity of RNA helicase hepatitis C by 57.90% and 27.55%. In addition, the protein was able to suppress the activity of Staphylococcus aureus ATCC 6538, E. coli EPEC K.1.1. and Salmonella typhii ATCC 25241. Activitiy of lectin was stable at 30 °C and was unaffected by the action of the enzyme. These results indicate that lectin of microalgae BTM 11 could be a alternative to antiviral and antibacterial proteins.
Optimization of Expression Condition, Two Dimensional And Melting Point-Based Characterization of Recombinant Human Interferon Alpha-2a Fusion and Non Fusion Forms Ningrum, Ratih Asmana; Wardhani, Widdya Kusuma; Wahyuni, Ike; Mustopa, Apon Zaenal
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2018.v22.n2.57-64

Abstract

     Recombinant Human Interferon Alpha-2a (rhIFNα-2a) is a therapeutic protein that used in hepatitis and cancer treatments. In our previous research, we developed higher molecular weight of the protein through human serum albumin fusion. The fusion and non fusion form of rhIFNα-2a were produced in Pichia pastoriswith 86 kDa and 19 kDa in size respectively. In previous research, protein yield was not reproducible due to unoptimized expression conditions. This reseach was aimed to optimize expression condition process and to characterize the fusion and non fusion forms of rhIFNα-2a. The parameters to observe in overproduction include nutrient (media and methanol concentration) and non nutrient (temperature andincubation period). Affinity and size exclusion cromatographicwere compared in protein purification. BCA assay was used to determine quantity of protein. Protein characterization was conducted using two-dimensional SDS PAGE and denaturation analyses. The optimal condition of expression was achieved using complex media with 1% of methanol for 3 day incubation period at 25°C. The protein yield was reproducible and higher comparing to previous research. Affinity chromatography resulted in higher purity of the proteins comparing to size exclusions. Characterization using two dimensional gel analysis revealed that isoelectric point of rhIFNα-2a is 6.5 for fusion form and 6.0 for non fusion form. The melting points of fusion protein were 56°C and 62°C whilst that of non fusion was 56°C.
Partial Purification, Characterization, and Application of Extracellular Aspartic Protease from Lactobacillus casei WSP in Producing the Bioactive Peptides with Antibacterial and Antioxidant Activity Solikhin, Akhmad; Mustopa, Apon Zaenal; Suharsono, Suharsono; Putranto, Wendry Setiyadi
ANNALES BOGORIENSES Vol 22, No 2 (2018): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2018.v22.n2.47-56

Abstract

   Lactobacillus casei WSP-derived an aspartic protease was sequentially purified by using chromatography gel filtration sephadex G-50. It resulted in a 22.81-fold increase of specific activity (51.5 U/mg) with a final yield of 1.9%. The estimated molecular weight of the purified enzyme was 37 kDa and showed gelatinolytic activity in zymogram assay. The enzyme exhibited optimum activity at 40ºC and pH 6 with casein as the substrate. Enzyme activity was significantly inhibited by pepstatin A (0.5 mM and 1 mM), confirming that this enzyme is a group of aspartic proteases, while other inhibitors such as EDTA, PMSF and iodoacetic acid showed no inhibition effect on the activity of enzyme. The addition of metal ion to the enzyme decreased enzyme activity, indicating the proteolytic enzyme was metal ion- dependent. Denaturant such as DDT tended to increase caseinolytic activity. Furthermore, this enzyme was capable of generating the new peptides from skimmed milk with the size 8 kDa, 10 kDa and 15 kDa. These peptides have potential as antibacterial and antioxidant agents.
Co-Authors Ai Hertati, Ai Akhmad Solikhin Akmaliyah, Rizna Alfisyahrin, Wida Nurul Amani, Febriyanti Nur Amelia, Suci Amelia, Suci Andi Asmawati Azis Anika Prastyowati, Anika Anja Meryandini Anna Ida Sunaryo Purwiyanto Arifah, Rosyida Khusniatul Ario Betha Juanssilfero Chairunnisa, Sheila Chihombori, Tatenda Calvin DWI SUSILANINGSIH Ekawati, Nurlaili Eva Johannes Farida, Hilda Farida, Hilda Fatimah fatimah Fatimah Fidien, Khadijah Alliya Fidien Firdaus, Moh Egy Rahman GINA KARTINA Harsi D. Kusumaningrum Hartati Chairunnisa Hartoni Hasim - Hasim Hasim Huda Shalahudin Darusman Hudaida Syahrumsyah, Hudaida Ikramullah, Muh. Chaeril Iman Rusmana Irawan, Herman Irawan, Shasmita Isworo, Rhestu Isworo, Rhestu Jendri Mamangkey Joko Wahyono, Daniel Kartika Sari Dewi Kusdianawati Kusmajadi Suradi Kustiariyah Tarman Kusumawati, Arizah LINDA SUKMARINI Lita Triratna Magdalena Litaay Maggy Thenawidjaja Suhartono Mala Nurilmala Manguntungi, Baso Maulidiani, Maulidiani Meilina, Lita Meiyerani, Jeni Melki Mustafawi, Wike Zahra Mustika Tuwo, Mustika Mutiara, Ilma Nina Herlina Novianti, Ela Nur Amani, Febriyanti Nur Umami, Rifqiyah Nurfatwa, Maritsa Pandayu, Iga Firmansyah Popi Hadi Wisnuwardhani, Popi Hadi Puspo Edi Giriwono Putri, Andini Setyanti Putri, Prabawati Hyunita Putri, Prabawati Hyunita Ramadhian, M. Zalfa RATIH ASMANA NINGRUM Ratna, Lita Tri Refli, Redoyan Rifqiyah Nur Umami, Rifqiyah Nur Rika Indri Astuti Saputri, Dinar Suksmayu Saputri Sofyana, Neng Tanty Sri Swasthikawati, Sri Suharli, Lili Suharsono Suharsono Surachma, Rahma Sari Tri Wibawa Trinugroho, Joko P Urnemi Urnemi, Urnemi Vanggi, Leggina Rezzy Vanggy, Leggina Rezzy Wahyuni, Ike Wahyuni, Ike Wardhani, Widdya Kusuma Wardhani, Widdya Kusuma Wendry Setiyadi Putranto Wibowo, Krisna Dwi Aria Wijaya, Hans Wike Ayu Eka Putri Yudi Purnomo