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Irawan, Herman
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Agriculture, Biological Sciences & Forestry Earth & Planetary Sciences

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Potential Probiotic Yeasts of the Pichia Genus Isolated from ‘Dadih’, a Traditional Fermented Food of West Sumatra, Indonesia Chihombori, Tatenda Calvin; Mustopa, Apon Zaenal; Astuti, Rika Indri; Mutiara, Ilma; Refli, Redoyan; Umami, Rifqiyah Nur; Fatimah; Irawan, Herman; Ekawati, Nurlaili; Trinugroho, Joko P; Akmaliyah, Rizna; Chairunnisa, Sheila; Amani, Febriyanti Nur; Manguntungi, Baso; Hertati, Ai; Mamangkey, Jendri
HAYATI Journal of Biosciences Vol. 32 No. 2 (2025): March 2025
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.32.2.320-340

Abstract

Fermented buffalo milk, known as dadih, serves as a reservoir of potential probiotic yeasts. Over the past two decades, probiotic yeasts have gained increasing attention in both basic and clinical sciences due to their health benefits. This study aimed to isolate and characterize probiotic yeasts from dadih. Yeasts were isolated using yeast Extract, peptone, and dextrose (YPD) medium, and molecularly identified through 18S-rRNA sequencing. Probiotic potential was assessed by evaluating resistance to acidic pH, bile salts, proteolytic, lipolytic, and hemolytic activities. Secondary metabolites produced during fermentation were tested for antimicrobial properties. GBT30 and GBT37 isolates were selected based on their superior performance in probiotic property assays for further analysis. Molecular identification revealed these isolates as Pichia occidentalis (GBT30) and Pichia kudriavzevii (GBT37). Both strains demonstrated in vitro survivability under simulated gastrointestinal conditions and exhibited antimicrobial activity. Whole-genome sequencing of P. kudriavzevii GBT37 identified a genome size of 10,906,850 base pairs, distributed across four chromosomes with a GC content of 38.26%. Notably, secondary metabolite biosynthesis genes were located on contig 7. In addition, 26 probiotic-related genes, including GSY1, HSC82, HSP104, TPS1, ARN1, FLO1, ALA1, SIR2, and others, were identified in P. kudriavzevii GBT37, indicating its potential as a probiotic yeast. The traditional fermentation process of dadih offers probiotic yeasts with promising health benefits, supporting its potential as a functional food.
Truncation on N-Terminal Hydrophobic Domain of L1 Major Capsid Protein of Human Papillomavirus Type 52 Enhances Its Expression in Hansenula polymorpha Arifah, Rosyida Khusniatul; Firdaus, Moh Egy Rahman; Chairunnisa, Sheila; Irawan, Shasmita; Ekawati, Nurlaili; Irawan, Herman; Nurfatwa, Maritsa; Hertati, Ai; Swasthikawati, Sri; Novianti, Ela; Mustafawi, Wike Zahra; Nur Umami, Rifqiyah; Mustopa, Apon Zaenal
HAYATI Journal of Biosciences Vol. 32 No. 4 (2025): July 2025
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.32.4.1062-1072

Abstract

Human papillomavirus (HPV) infection is the main cause of cervical cancer. The administration of the HPV prophylactic vaccine, which is commonly produced based on HPV L1 major capsid protein, significantly reduces the incidence of cervical cancer. However, the coverage of the HPV vaccination program is often hindered due to its relatively high cost. This study aimed to evaluate the impact of N-terminal hydrophobic domain truncation on the expression of L1 major capsid protein of HPV type 52 in Hansenula polymorpha. The truncation enhanced the yield of L1 protein expression compared with the full length, which was confirmed by Western blot and ELISA. Furthermore, the truncated L1 protein formed virus-like particles (VLPs), which were confirmed by transmission electron microscopy (TEM). Bioinformatics analysis showed that the truncated L1 protein was more soluble compared with the full length, possibly increasing the protein expression. These findings could pave the way for the development of a more cost-effective HPV type 52 L1 protein production in H. polymorpha to be used as a VLP-based prophylactic vaccine.
Medium Optimization for Recombinant Human Papillomavirus Type 52 L1 Protein Production in Pichia pastoris GS115 Platform on Bioreactor Scale Mustopa, Apon Zaenal; Nur Amani, Febriyanti; Irawan, Herman; Novianti, Ela; Swasthikawati, Sri; Ekawati, Nurlaili; Nurfatwa, Maritsa; Joko Wahyono, Daniel; Juanssilfero, Ario Betha; Mamangkey, Jendri; Purnomo, Yudi; Hertati, Ai; Wijaya, Hans; Dewi, Kartika Sari; Ningrum, Ratih Asmana
HAYATI Journal of Biosciences Vol. 32 No. 5 (2025): September 2025
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.32.5.1283-1294

Abstract

Human papillomavirus (HPV) stands as the primary etiological agent in the development of invasive cervical cancer worldwide. The L1 protein is a pivotal constituent of prophylactic HPV vaccines. Notably, HPV type 52 is one of the most prevalent genotypes found in squamous cell carcinoma cases in Indonesia. This research endeavor aims to enhance the productivity of recombinant HPV-52 L1 protein by optimizing the culture conditions of P. pastoris GS115 cells. In this study, we conducted trials employing 17 different media variants to optimize the expression of recombinant HPV-52 L1 protein. The results from small-scale experiments revealed three media, namely SYN6.10, BMMY, and SYN6.1, which exhibited promising yields of recombinant HPV-52 L1 protein as assessed through ELISA or immunoassay analysis. We succeeded in refining the SYN6.10 derivative, denoted as SYN6.10b, specifically designed for use in 1-L and 5-L bioreactors. This achievement was realized by adjusting Trace Element Solution (TES) and Vitamin Solution (VS) concentrations and implementing a methanol fed-batch phase with the addition of 0.3% methanol after 24 and 48 hours of fermentation in the P. pastoris medium. Further visualizations through SDS-PAGE and western blot analysis confirmed the protein after 72 hours of fermentation in a 1-L bioreactor using the SYN6.10b medium. In conclusion, the SYN6.10b medium required a 72 hours fermentation period to successfully express recombinant HPV-52 L1 protein in the P. pastoris platform.
Co-Authors Ai Hertati, Ai Akmaliyah, Rizna Amani, Febriyanti Nur Apon Zaenal Mustopa Arifah, Rosyida Khusniatul Ario Betha Juanssilfero Chairunnisa, Sheila Chihombori, Tatenda Calvin Ekawati, Nurlaili Fatimah Firdaus, Moh Egy Rahman Irawan, Shasmita Jendri Mamangkey Joko Wahyono, Daniel Kartika Sari Dewi Manguntungi, Baso Mustafawi, Wike Zahra Mutiara, Ilma Novianti, Ela Nur Amani, Febriyanti Nur Umami, Rifqiyah Nurfatwa, Maritsa RATIH ASMANA NINGRUM Refli, Redoyan Rifqiyah Nur Umami, Rifqiyah Nur Rika Indri Astuti Sri Swasthikawati, Sri Trinugroho, Joko P Wijaya, Hans Yudi Purnomo