Apon Zaenal Mustopa
Research Center for Biotechnology, Indonesian Institute of Sciences Jalan Raya Bogor km 46, Cibinong 16911, Bogor, Indonesia

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Antioxidant and Cytotoxic Activities of Lactic Acid Bacteria on Colorectal Cancer WiDr Cell Line Wisnuwardhani, Popi Hadi; Ningrum, Ratih Asmana; Mustopa, Apon Zaenal; Vanggi, Leggina Rezzy; Kusdianawati, Kusdianawati Kusdianawati
Indonesian Journal of Cancer Chemoprevention Vol 12, No 1 (2021)
Publisher : Indonesian Society for Cancer Chemoprevention

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14499/indonesianjcanchemoprev12iss1pp28-36

Abstract

Colorectal cancer (CRC) is one of the leading causes of cancer and cancer-related deaths worldwide. Lactic acid bacteria (LAB) are bacteria that have potential activity as an inhibitor of the growth of colorectal cancer, and also has been widely used and was very useful for consumption. In our previous study, we isolated various LAB from Indonesian traditional fermented food. This study aims to determine the potential of LAB as an anticancer agent by determining the antioxidant activity and cytotoxicity assay of colon cancer in the WiDr cell line. This study used extracellular extract of various LAB. We use the Diphenylpicrylhydrazyl (DPPH) method to determine the antioxidant activity and 3-(4,5'dimethylihiazol-2-yl),2.5-di-phenyl-relrrzolium bromid (MTT) assay to study cytotoxicity activity. The viability cell staining also applied to detect unviable cells. The results informed that the highest antioxidant activity was shown by S.34 LAB with 81% activity. The S.34 also showed cytotoxicity activity with 73% of WiDr viable cell at a concentration of 200 μg/mL of LAB extract. Based on the results of the study, it can be concluded that the S.34 LAB from Bekasam may inhibit the proliferation of WiDr cell lines and It had the highest antioxidant activity comparing to other LAB samples.Keywords: Lactic Acid Bacteria, colorectal cancer, anticancer, antioxidant, WiDr cells.
The Purification of Rennin-Like Protease from Lactobacillus paracasei Isolated from Ettawa Goat Milk Putranto, Wendry Setiyadi; Mustopa, Apon Zaenal; Kusumawati, Arizah; Prastyowati, Anika
Annales Bogorienses Vol. 24 No. 2 (2020): Annales Bogorienses
Publisher : BRIN

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Abstract

There is a protease produced by bateria that has characteristics similar to rennin from a calf. Rennin has the ability to clot casein in milk. Rennin-like protease (RLP) is produced by bacteria extracellularly. Lactic Acid Bacteria (LAB) have the potential to be developed for RLP production because they are safe and non-pathogenic bacteria. Rennin is needed in the process of milk coagulation to subsequently obtain a curd in the process of making cheese. In this study, the LAB isolated from Ettawa goat milk (isolate 2.12) which produced RLP was 99% identical to Lactobacillus paracasei based on 16S rRNA gene sequence analysis. The purification of the RLP L. paracasei 2.12 with 60% ammonium sulfate deposition, dialysis, and filtration gel chromatography Sephadex G-50 showed a single 38 kDa protein band with SMCA/SPA was 4.48 higher than that of the calf rennet with a ratio value of 1, therefore in this study, RLP L. paracasei 2.12 was developed as an alternative to renin in cheese making.
Antidiabetic, Antioxidants and Antibacterial Activities of Lactic Acid Bacteria (LAB) from Masin (Fermented Sauce from Sumbawa, West Nusa Tenggara, Indonesia) Manguntungi, Baso; Vanggy, Leggina Rezzy; Fidien, Khadijah Alliya Fidien; Saputri, Dinar Suksmayu Saputri; Mustopa, Apon Zaenal; Ekawati, Nurlaili; Nurfatwa, Maritsa; Prastyowati, Anika; Irawan, Shasmita
Annales Bogorienses Vol. 24 No. 1 (2020): Annales Bogorienses
Publisher : BRIN

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Abstract

The study aimed to determine the effectiveness of metabolites from Lactic Acid Bacteria (LAB) derived Masin (fermented sauce from Sumbawa) as antioxidant, antidiabetic, and antibacterial compounds. The LAB isolates were isolated from various strains of Staphylococcus piscifermentan which consisted of Staphylococcus piscifermentans strain CIP103958 (code: 2), strain BULST54 (code: 17), strain SK03 (code: 11), strain ATCC 51136 (code: 34), strain PCM 2409 (code: 28) and strain PU-87 (code: 5). The Metabolites of LAB were analyzed by the bioprospecting test to indicate antidiabetic, antioxidant and antibacterial activities. The isolate (Code: 5) at 500 ug/ml showed the most effective antioxidant activity up to 71%. The isolate (code: 28), at 300 ug/ml revealed to have the most antidiabetic activity up to 43 %. The isolate (code: 2) showed moderate antibacterial activity with the inhibition zone of 5.59 mm. The results of the antidiabetic, antioxidant and antibacterial activity showed that the secondary metabolites produced by LAB from the Masin have broad activities as an antidiabetic, antioxidant and antibacterial.
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 : BRIN

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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.
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 : BRIN

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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.
Antioxidant, Antibacterial, and Antidiabetic Activities of Roselle (Hibiscus sabdariffa) Extracts Suharli, Lili; Manguntungi, Baso; Azis, Andi Asmawati; Mustopa, Apon Zaenal; Meilina, Lita; Pandayu, Iga Firmansyah; Vanggy, Leggina Rezzy; Irawan, Shasmita
Annales Bogorienses Vol. 25 No. 2 (2021): Annales Bogorienses
Publisher : BRIN

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Abstract

Hibiscus sabdariffa L., also referred to as roselle, is commonly utilized in the pharmaceutical and food industries. Roselle contains bioactive compounds such as phenolics, alkaloids, tannins, flavonoids, saponins, and organic acids, which have pharmacological properties, such as antioxidant, antibacterial, immune booster, antidiabetic, anti-inflammatory, and anti-hypertensive properties. There are many studies regarding the pharmacological activities of roselle extract and its applications. However, there has been no research to study the effectiveness of the solvent in testing roselle petal extracts against antibacterial, antioxidant, and antidiabetic activities, simultaneously. This research used two kinds of polar solvents, dH2O and ethanol, with various concentrations for antibacterial activity test by five pathogenic bacteria, for antioxidant test by the DPPH method, and for antidiabetic test by the alpha-glucosidase inhibition method. The result showed that the ethanol extract of roselle had higher antibacterial activity compare to the roselle water extract. Antioxidant activity of roselle ethanol extract at 20% concentration had the highest activity 69.75 ± 0.002%; while, the 100% concentration of roselle water extract had the highest antioxidant activity 138.73 ± 0.013%. antidiabetic activity of roselle ethanol and water extract at 100% concentration had the highest activity 1,195.44 ± 0.007% and 1,552.49 ± 0.069%, respectively.
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 : BRIN

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Abstract

BTM 11 is unknown species of microalgae which has active compounds that can inhibit viruses. Lectin is a carbohydrate-binding protein that is found in microalgae with antiviral and antibacterial activities. The purpose of this study was to perform identification, isolation, characterization, and assay of lectin inhibitory activity of microalgae BTM 11. The result shows that microalgae BTM 11 has homology with Cyanobacterium (99%) and Geitlerinema sp (98%). Lectin of microalgae BTM 11 has 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 unaffected by the action of the enzyme. These results indicate that lectin of microalgae BTM 11 could be an alternative to antiviral and antibacterial proteins.
Enterococcus faecium 1.15 Isolated from Bakasam Showed Milk Clotting Activity Putranto, Wendry Setiyadi; Suradi, Kusmajadi; Chairunnisa, Hartati; Mustopa, Apon Zaenal; Kusumaningrum, Harsi Dewantari; Suhartono, Maggy Thenawidjaja
Annales Bogorienses Vol. 21 No. 1 (2017): Annales Bogorienses
Publisher : BRIN

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Abstract

Rennin-like protease of many microorganisms behave similarly to chymosin and are potential alternatives of rennet. The lactic acid bacteria with milk clotting activity were isolated from Bakasam, an Indonesian traditional fermented meat. Screening assay 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% identical with Enterococcus faecium. The isolate potentially produced renin-like protease to subtitute renin from veal.
Preclinical Evaluation of HPV Type 52 L1L2 Chimeric Protein as a Cervical Cancer Vaccine Candidate Sari, Isti Kartika; Pamungkas, Joko; Mustopa, Apon Zaenal; Wibawan, I Wayan Teguh; Mamangkey, Jendri; Chairunnisa, Sheila; Irawan, Herman; Hertati, Ai; Ekawati, Nurlaili; Umami, Rifqiyah Nur; Novianti, Ela; Nurfatwa, Maritsa; Darusman, Huda Shalahudin
HAYATI Journal of Biosciences Vol. 33 No. 3 (2026): May 2026
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.33.3.556-565

Abstract

High-risk human papillomaviruses (HPVs) are the primary etiological agents of cervical cancer, accounting for more than 300,000 deaths annually worldwide. Current prophylactic vaccines based on recombinant L1 major capsid virus-like particles (VLPs) have demonstrated strong efficacy but are restricted to a limited spectrum of HPV types. To address this limitation, the present study evaluated a recombinant L1L2 chimeric protein derived from HPV type 52 as a potential candidate for a broad-spectrum vaccine. The chimeric protein was expressed in Escherichia coli strain BL21 (DE3) and purified for immunization studies. Female BALB/c mice (Mus musculus, n = 5 groups) were immunized, and immune responses were analyzed by enzyme-linked immunosorbent assay (ELISA) and pseudovirion-based neutralization assays (PBNA). The recombinant L1L2 vaccine candidate induced detectable antibody responses against HPV antigens; however, neutralizing activity remained modest. Histopathological analysis of liver and kidney tissues showed no evidence of toxicity, supporting the safety profile of the candidate. In summary, these results suggest that the HPV type 52 L1L2 chimeric protein represents a promising platform for the development of cervical cancer vaccines, although further optimization is required to achieve robust cross-neutralizing efficacy.
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 I wayan Teguh Wibawan Ikramullah, Muh. Chaeril Iman Rusmana Irawan, Herman Irawan, Shasmita Isworo, Rhestu Isworo, Rhestu Jendri Mamangkey Joko Pamungkas 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 Sari, Isti Kartika 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