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All Journal Journal of Tropical Life Science : International Journal of Theoretical, Experimental, and Applied Life Sciences Annales Bogorienses
Anika Prastyowati, Anika
Fak. Teknobiologi Univ. Atmajaya Yogyakarta
Agriculture, Biological Sciences & Forestry Environmental Science

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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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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.
Codon Optimization and Epitope Identification of L1 Protein Human Papillomavirus Type 52 for Expression in Lactococcus lactis: Codon Optimization and Epitope Identification L1 Protein HPV52 Prastyowati, Anika; Hakim, Mohamad Saifudin; Wijayanti, Nastiti; Wibawa, Tri
Journal of Tropical Life Science Vol. 15 No. 3
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/jtls.15.03.03

Abstract

Human papillomavirus (HPV) type 52 is among the top three high-risk oncogenic types that are associated with cervical cancer worldwide, especially in Indonesia. Designing a vaccine against HPV using an Lactococcus lactis expression system is a promising strategy, as this bacterium is well-known for its probiotic properties and can be safely utilized as a delivery carrier for oral vaccines. This study aimed to optimize the codon usage of the L1 protein of HPV type 52 for expression in L. lactis expression system and to identify potential epitopes using bioinformatics tools. To determine the codon optimization, the L1 protein sequence of HPV type 52 was retrieved from the National Center for Biotechnology Information (NCBI) database. Furthermore, codon optimization was conducted once the model had been established using OPTIMIZER, Clustal Omega, Restriction Mapper, and the ExPASy tool, based on L. lactis. The final construct was predicted to have a B-cell epitope by Ellipro tools, antigenicity by VaxiJen v.2.0, allergenicity by AllerTOP v.2.0, and toxicity by ToxIBTL. This resulted in a potential vaccine candidate with a Codon Adaptation Index (CAI) of 0.754 and GC content of 39.0%. Identification of epitopes from the optimized gene resulted in two peptide sequences, WRPSEATVYLPPVPVSKVVS and GTLGDPVPGDLYIKGSNSGNTATVQ, as components of the vaccine candidate.
Co-Authors Apon Zaenal Mustopa Ekawati, Nurlaili Fidien, Khadijah Alliya Fidien Hakim, Mohamad Saifudin Irawan, Shasmita Kusumawati, Arizah Manguntungi, Baso Nastiti Wijayanti Nurfatwa, Maritsa Saputri, Dinar Suksmayu Saputri Tri Wibawa Vanggy, Leggina Rezzy Wendry Setiyadi Putranto