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Apon Zaenal Mustopa
Research Center for Biotechnology, Indonesian Institute of Sciences (LIPI)

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The Purification of Rennin-Like Protease from Lactobacillus paracasei Isolated from Ettawa Goat Milk Wendry Setiyadi Putranto; Apon Zaenal Mustopa; Arizah Kusumawati; Anika Prastyowati
Annales Bogorienses Vol. 24 No. 2 (2020): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2020.v24.n2.74-80

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) Baso Manguntungi; Leggina Rezzy Vanggy; Khadijah Alliya Fidien Fidien; Dinar Suksmayu Saputri Saputri; Apon Zaenal Mustopa; Nurlaili Ekawati; Maritsa Nurfatwa; Anika Prastyowati; Shasmita Irawan
Annales Bogorienses Vol. 24 No. 1 (2020): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2020.v24.n1.27-34

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 Akhmad Solikhin; Apon Zaenal Mustopa; Suharsono Suharsono; Wendry Setiyadi Putranto
Annales Bogorienses Vol. 22 No. 2 (2018): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

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.
Optimization of Expression Condition, Two Dimensional And Melting Point-Based Characterization of Recombinant Human Interferon Alpha-2a Fusion and Non Fusion Forms Ratih Asmana Ningrum; Widdya Kusuma Wardhani; Ike Wahyuni; Apon Zaenal Mustopa
Annales Bogorienses Vol. 22 No. 2 (2018): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

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.
Molecular Identification of Microalgae BTM 11 and its Lectin Isolation, Characterization, and Inhibition Activity Apon Zaenal Mustopa; Rhestu Isworo; Mala Nurilmala; Dwi Susilaningsih
Annales Bogorienses Vol. 20 No. 2 (2016): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2016.v20.n2.47-54

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 Wendry Setiyadi Putranto; Kusmajadi Suradi; Hartati Chairunnisa; Apon Zaenal Mustopa; Harsi Dewantari Kusumaningrum; Maggy Thenawidjaja Suhartono
Annales Bogorienses Vol. 21 No. 1 (2017): Annales Bogorienses
Publisher : National Research and Innovation Agency (BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2017.v21.n1.9-14

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.
Co-Authors Akhmad Solikhin Anika Prastyowati Arizah Kusumawati Baso Manguntungi Dinar Suksmayu Saputri Saputri Dwi Susilaningsih Giriwono , Puspo Edi Harsi D. Kusumaningrum Harsi Dewantari Kusumaningrum Hartati Chairunnisa Hartati Chairunnisa Ike Wahyuni Khadijah Alliya Fidien Fidien Kusmajadi Suradi Kusmajadi Suradi Leggina Rezzy Vanggy Maggy Thenawidjaja Suhartono Maggy Thenawidjaja Suhartono Mala Nurilmala Maritsa Nurfatwa Nurlaili Ekawati Ratih Asmana Ningrum Rhestu Isworo Shasmita Irawan Suharsono Suharsono Wendry Setiyadi Putranto Wendry Setiyadi Putranto Wendry Setiyadi Putranto Widdya Kusuma Wardhani