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All Journal International Journal of Advances in Applied Sciences Journal of Tropical Life Science : International Journal of Theoretical, Experimental, and Applied Life Sciences Agrotekno Buletin Udayana Mengabdi Agrointek Indonesian Green Technology Journal Media Ilmiah Teknologi Pangan (Scientific Journal of Food Technology) Indonesian Journal of Biotechnology Jurnal Teknologi & Industri Hasil Pertanian Jurnal Pascapanen dan Bioteknologi Kelautan dan Perikanan Teknologi Indonesia Canrea Journal: Food Technology, Nutritions, and Culinary Journal Jurnal Gastronomi Indonesia AJARCDE (Asian Journal of Applied Research for Community Development and Empowerment) SEAS (Sustainable Environment Agricultural Science) Seminar Ilmiah Nasional Teknologi, Sains, dan Sosial Humaniora (SINTESA) JURNAL REKAYASA DAN MANAJEMEN AGROINDUSTRI Jurnal Ilmiah Teknologi Pertanian Agrotechno Metamorfosa: Journal of Biological Science Open Access DRIVERset Itepa : Jurnal Ilmu dan Teknologi Pangan
Ida Bagus Wayan Gunam
Program Studi Teknologi Industri Pertanian, Fakultas Teknologi Pertanian, Universitas Udayana, Badung, Bali, Indonesia
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemistry Computer Science & IT Control & Systems Engineering Decision Sciences, Operations Research & Management Earth & Planetary Sciences Education Energy Engineering Environmental Science Health Professions Immunology & microbiology Industrial & Manufacturing Engineering Materials Science & Nanotechnology Mathematics Physics Social Sciences Other

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The Selection and the Growth Condition Optimization of Ethanol‐Producing Microbes Isolated from Ragi Tapai: Selection and the Growth Condition Optimization of Ethanol‐Producing Microbes Ida Bagus Wayan Gunam; I Gede Arya Sujana; I Made Mahaputra Wijaya; Yohanes Setiyo; I Wayan Arnata; I Wayan Wisma Pradnyana Putra
Journal of Tropical Life Science Vol. 13 No. 2 (2023)
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/jtls.13.02.12

Abstract

Ethanol is a biofuel produced from renewable resources, which potentially plays an important role in solving future fuel problems. This study aimed to select the highest ethanol-producing isolate from candidates obtained from previously isolated candidates from ragi and cassava tapai. The selection process was conducted in 2 stages, namely: 1) Selection of the highest ethanol-producing isolate from seven isolate candidates using PYG media containing peptone, yeast extract, and glucose at 0.75%, 0.75%, and 15%, respectively and was followed by: 2) Optimization of the growth conditions of the highest ethanol-producing isolate, which was conducted at various temperatures of 27, 30, 33, 35, 37, and 40°C with the combination of various pH of 3.5, 4.5, 5.5, and 6.5. The experimental results showed that the R5I3 isolate was the highest ethanol-producing performance isolate, which yielded approximately 4.69±0.25% (v/v). Following the temperature and pH optimization of the fermentation processes, the optimum growth conditions were at 35°C and pH 5.5, where the ethanol produced was increased to 8.63 ± 0.04% (v/v). With these results, this new strain has the potential to be used in bioethanol production processes and other industrial applications.
Exploring Microbial Diversity in Green Honey from Pulau Banggi Sabah: A Preliminary Study: Microbial Diversity in Green Honey from Pulau Banggi Sabah Rajindran, Nanthini; Ab Wahabb, Roswanira; Huda , Nurul; Adekilekun Oyewusi, Habeebat; Wayan Gunam, Ida Bagus; Mohd Shariff , Amir Husni; Izzah Ismail, Norjihada; Huyop, Fahrul
Journal of Tropical Life Science Vol. 14 No. 1 (2024)
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/jtls.14.01.02

Abstract

The microbiological composition of honey can include microorganisms that are beneficial or harmful to human health. Therefore, it is essential to investigate the microbiological quality of different honey types available in the market. However, there is limited information available on the analysis, isolation, and characterization of honey-associated microbes, especially for green honey from Banggi Island. Green honey is sourced from underground areas within the island's forest. This study aimed to assess the microbiological quality of raw (freshly collected) and processed green honey by examining the presence of bacteria, yeast, molds, and pathogens. The results revealed that raw green honey had a slightly higher total plate count (770 ± 0.03 cfu/g) compared to processed green honey (640 ± 0.02 cfu/g). Both raw and processed green honey contained Lactobacillus spp. with counts of 350 ± 0.02 cfu/g and 160 ± 0.02 cfu/g, respectively. Bacillus count was higher in raw green honey (110 ± 0.01 cfu/g) compared to processed green honey (5 ± 0.01 cfu/g). Molds were only detected in raw green honey, while osmophilic yeast counts were higher in raw green honey (16000 ± 0.03 cfu/g) compared to processed green honey (120 ± 0.02 cfu/g). Mesophilic bacteria, thermophilic bacteria, coliforms, E. coli, and Staphylococcus aureus were not detected in either raw or processed green honey. Furthermore, green honey was free from pathogenic bacteria such as Salmonella spp., Listeria spp., and Shigella spp. Bacteria isolated from green honey included Lysinibacillus macrolides, Lysinibacillus boronitolerans, Paenibacillus cineris, Paenibacillus favisporus, and Bacillus oleronius, none of which were pathogenic. This study identified important microorganisms present in green honey, which have the potential to provide beneficial effects without posing any harm to human health.
Exploring Microbial Diversity in Green Honey from Pulau Banggi Sabah: A Preliminary Study: Microbial Diversity in Green Honey from Pulau Banggi Sabah Rajindran, Nanthini; Ab Wahabb, Roswanira; Huda , Nurul; Adekilekun Oyewusi, Habeebat; Wayan Gunam, Ida Bagus; Mohd Shariff , Amir Husni; Izzah Ismail, Norjihada; Huyop, Fahrul
Journal of Tropical Life Science Vol. 14 No. 1 (2024)
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/jtls.14.01.02

Abstract

The microbiological composition of honey can include microorganisms that are beneficial or harmful to human health. Therefore, it is essential to investigate the microbiological quality of different honey types available in the market. However, there is limited information available on the analysis, isolation, and characterization of honey-associated microbes, especially for green honey from Banggi Island. Green honey is sourced from underground areas within the island's forest. This study aimed to assess the microbiological quality of raw (freshly collected) and processed green honey by examining the presence of bacteria, yeast, molds, and pathogens. The results revealed that raw green honey had a slightly higher total plate count (770 ± 0.03 cfu/g) compared to processed green honey (640 ± 0.02 cfu/g). Both raw and processed green honey contained Lactobacillus spp. with counts of 350 ± 0.02 cfu/g and 160 ± 0.02 cfu/g, respectively. Bacillus count was higher in raw green honey (110 ± 0.01 cfu/g) compared to processed green honey (5 ± 0.01 cfu/g). Molds were only detected in raw green honey, while osmophilic yeast counts were higher in raw green honey (16000 ± 0.03 cfu/g) compared to processed green honey (120 ± 0.02 cfu/g). Mesophilic bacteria, thermophilic bacteria, coliforms, E. coli, and Staphylococcus aureus were not detected in either raw or processed green honey. Furthermore, green honey was free from pathogenic bacteria such as Salmonella spp., Listeria spp., and Shigella spp. Bacteria isolated from green honey included Lysinibacillus macrolides, Lysinibacillus boronitolerans, Paenibacillus cineris, Paenibacillus favisporus, and Bacillus oleronius, none of which were pathogenic. This study identified important microorganisms present in green honey, which have the potential to provide beneficial effects without posing any harm to human health.
In silico Characterization of Poly (ethylene) Terephthalate (PET): Degrading Enzymes from Rhizobacter sp. for Enzymatic Degradation Mechanisms: Characterization of Rhizobacter sp. PET Hydrolases Damuri, Nur Wahida; Mohd Rozdhi, Amira Azawani; Tirmizhi Abubakar, Munkaila; Wayan Gunam, Ida Bagus; Huyop, Fahrul; Oyewusi, Habeebat Adekilekun
Journal of Tropical Life Science Vol. 15 No. 1 (2025)
Publisher : Journal of Tropical Life Science

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

Abstract

Dienelactone hydrolase (DHL) from Rhizobacter sp. is an enzyme from the β‐ketoadipate pathway that belongs to the α/β hydrolase family. It involves the conversion of chloroaromatics, such as nitrophenols and hydrocarbons, into harmless metabolites. The sequence-based analysis of Dienelactone hydrolase from Rhizobacter sp. shows significant homology to the extensively studied polyethylene terephthalate hydrolase of Ideonella sakaiensis (IsPETase). IsPETase can degrade the polymer, polyethylene terephthalate (PET), at room temperature. It was chosen as a template for dienelactone hydrolase from Rhizobacter sp. that was studied as a putative PET hydrolase. This study employs bioinformatics tools such as Expasy Protparam, Clustal Omega, SWISS-MODEL, GROMACS and Autodock vina to analyse the amino acid sequence of this enzyme, predict its three-dimensional structure and study its binding interaction. The structure of the putative PET hydrolase has been determined with 0.9 GMQE value and an overall quality factor of 96%. The residues responsible in substrate binding interactions are Leu88, Ser160 and Trp185. Thus, this in silico analysis depicts the ability of the putative PET hydrolase to bind to the polymer polyethylene terephthalate.
Structural Comparison of α-agarase (α-AgaD) from Thalassomonas sp. LD5: An in-silico study: Structural Comparison of α-agarase (α-AgaD) from Thalassomonas sp. LD5 Oyewusi, Habeebat Adekilekun; Oladipo, Oluwatosin; Abdul Wahab, Roswanira; Adekilekun , Habeebulahi Ajibola; Wayan Gunam, Ida Bagus; Huyop, Fahrul
Journal of Tropical Life Science Vol. 15 No. 2
Publisher : Journal of Tropical Life Science

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

Abstract

The significance of agarase enzymes spans various high-value industries, including food, cosmetics, and medicine. These enzymes play a crucial role in the hydrolysis of agar to produce bioactive oligosaccharides, enabling wide-ranging applications across multiple fields. Among them, α-AgaD is a novel α-agarase enzyme produced by the Thalassomonas sp. LD5 strain. However, the structural and functional characteristics of α-AgaD within biological systems remain largely unexplored. This study therefore aims to provide a comprehensive in silico analysis of α-AgaD, focusing on its physicochemical properties, phylogenetic relationships, secondary structure composition, and 3D homology modelling. A range of computational tools was employed to validate the findings and enhance the structural understanding of this newly identified α-AgaD enzyme. The α-AgaD protein consists of 1,466 amino acids with a molecular weight of 158,787.82 Da. It has a theoretical isoelectric point (pI) of 4.14, indicating an overall acidic nature. Structural analysis revealed that alpha helices and random coils are the predominant secondary structures. Hydrophobic amino acids were more abundant than hydrophilic ones, with glycine accounting for approximately 10.4% of the total residues. The protein's aliphatic index was 72.05, and the instability index was 28.28, suggesting that α-AgaD is stable and likely to maintain its structure across a wide temperature range. Three-dimensional models of α-AgaD were constructed using I-TASSER, NCBI-PDB, SWISS-MODEL, and AlphaFold2, and subsequently validated using ERRAT, Verify3D, and PROCHECK. Among the models generated, AlphaFold2 produced the most accurate prediction, with nearly all amino acid residues located in the preferred regions of the Ramachandran plot. This further confirmed the reliability and quality of the refined models. The in silico structural analysis of α-AgaD offers valuable insights into the enzyme’s primary sequence, functional domains, and overall structural architecture, enhancing our understanding of α-agarase from Thalassomonas sp. LD5.
Concerted Structural analysis predictions of an organohalide pollutants uptake enzyme, putative permease protein (DehHsAADcPt) from Halomonas smyrnensis AAD6T.: Comparative Structural Prediction of putative permease protein (DehHsAADcPt) Oyewusi, Habeebat Adekilekun; Oladipo, Oluwatosin; Adekilekun, Habeebulahi; Abdul Wahab, Roswanira; Akinyede, Kolajo; Oladimeji Tugbobo, Samuel; Wayan Gunam, Ida Bagus; Huyop, Fahrul
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.15.03.07

Abstract

Halomonas smyrnensis AAD6T is a halophilic bacterium capable of utilizing haloalkanoic acid and possessing a specific gene for the uptake of organohalide pollutants. This distinctive characteristic has garnered the attention of researchers who seek to understand the underlying mechanisms. Among its genome, a putative permease protein known as DehHsAADcPt has been identified as a potential candidate for facilitating the uptake of these pollutants. Structural predictions of DehHsAADcPt have been conducted to gain a better understanding of its potential role in pollutant uptake. The predictions of DehHsAADcPt's structural characteristics, presented in this study, shed light on its potential application in bioremediation efforts. The implications of these findings are discussed in detail. The in-silico characterization and functional analysis of DehHsAADcPt was carried out with different bio-computational tools or servers. DehHsAADcPt belongs to the ABC inner membrane transporter permease family protein that is highly basic, hydrophobic, and thermostable having a molecular weight of 58,885.47Da as revealed from ExPASy server. The DehHsAADcPt compost mostly alpha helix structure and functional motif belongs to the binding-protein-dependent transport system inner membrane components and phage shock protein family. The 3-D structure obtained by AlphaFold2 homology modeling program and verified by Ramachandran plot revealed that most of the residues are in the allowed or favored regions of the plot. Likewise, several amino acid residues are predicted as ligand binding residues and most of them are highly conserved. The different computational tools used have proven to give holistic structural analysis predictions of DehHsAADcPt and revealed the concerted nature of these tools in elucidation. This study provides valuable insights into the structural and functional properties of DehHsAADcPt protein, which could pave the way for its potential application in the bioremediation of halogenated organic pollutants.
Co-Authors A.A.S. A. Sukmaningsih Ab Wahabb, Roswanira Abdul Wahab, Roswanira Adekilekun , Habeebulahi Ajibola Adekilekun Oyewusi, Habeebat Adekilekun, Habeebulahi Akinyede, Kolajo Ambar Kusumaningrum Amna Hartiati Anak Agung Made Dewi Anggreni Azis Akbar Hakim Bambang Admadi Harsojuwono Bimby Issassam Cokorda Anom Bayu Sadyasmara Damuri, Nur Wahida Deddy Setiadi Kadir Madjid Desi N. I. Izzabilah Dwi Ayu Kirani Paramita Dylla Hanggaeni Dyah Puspaningrum Ella Dewi Yusnia ENIEK KRISWIYANTI Erlangga, Muhammad Agung Fitra Ayu Sitanggang G.P. Ganda Putra Gde Agung Bagus Surya Adnyana Gede Bagus Suwarrizki G. P Hamonangan Sipayung Huda , Nurul Huyop, Fahrul I B. K. Widnyana Yoga I B. K. Widnyana Yoga I Dewa Gde Mayun Permana I Dewa Putu Rega Elyana I Gede Arya Sujana I Gede Arya Sujana I Gede Arya Sujana I Gede Krisna Putra Pratama I Gusti Ayu Lani Triani I Gusti Ayu Lani Triani I Gusti Bagus Ananta Wijaya Putra I Gusti Ngurah Agung Paranatha I Kadek Adi Wijaya Putra I Ketut Satriawan I Komang Trikuti I M. Mahaputra Wijaya I M. Mahaputra Wijaya I M. Mahaputra Wijaya I M. Mahaputra Wijaya I Made Griya Adi Parta I Made Mahaputra Wijaya I Made Mahaputra Wijaya I Made Mahaputra Wijaya I Made Mahaputra Wijaya I Made Sugitha I MADE SUPARTHA UTAMA I Made Supartha Utama I Made Yoga Saputra I MADE YOGA SEMARA GUNA I Putu Hendra Prasetya I W Suarta I W W Aryanika I W. Wisma P Putra I W. Wisma P. Putra I W.G. SEDANA YOGA I Wayan Arnata I Wayan Arnata I Wayan Arnata I Wayan Kasa I Wayan Suarta I Wayan Widia I Wayan Wisma Pradnyana Putra I Wayan Wisma Pradnyana Putra I.M.S. Wijaya IDA AYU ASTARINI Ida Ayu E. P. Wulandari Ida Ayu Pridari Tantri Ida Bagus Gede Brahmantara IDA BAGUS N. SURYA DARMA Ida Bagus Wisnu Matra Atmaja Indah S. R. Naibaho Indah Sri Rejeki Naibaho Izzah Ismail, Norjihada Jamas Prameshwari Janurianti , Ni Made Defy Janurianti, Ni Made Defy Ketut Agus Ary Subakti KETUT BUDA KOMANG AYU NOCIANITRI Kozo Asano Luh Dian Rna Fajarini Luh Putu Wrasiati Lutfi Suhendra Made Ria Defiani Mahaputra Wijaya Mertayasa, I Made Michael Jordi Theofanny Mohd Rozdhi, Amira Azawani Mohd Shariff , Amir Husni Monalisa Nababan Monikasari, Ni Nyoman Trisa Muhammad Iqbal N.P.I. Widyantari Nebay Cronika Simbolon Ni Kadek Eni Juniantari Ni Made Ayu Suardani Singapurwa Ni Made Ratih Despianti Ni Made Wartini Ni Putu Puspadi Aristyanti Ni Putu Suwariani Ni Wayan Wisaniyasa Noval Wahyu Adi Nursatria Purba Nurul Octavia Wasis NYOMAN SEMADI ANTARA Odilia Keron Oladimeji Tugbobo, Samuel Oladipo, Oluwatosin Oyewusi, Habeebat Adekilekun Pande Ketut Diah Kencana Pande Komang Suparyana Pavalee Chompoorat Tridtitanakiat Purnami, Ni Gusti Ayu Kade Sintya Ari Putu Agus Nadiarta Putu Ari Sandhi Wipradnyadewi - Putu Diah Wahyuni Putu Setia Budi Rajindran, Nanthini Rendy Sinaga Rike Pratiwi Sadyasmara, Cokorda Anom Bayu Sandhi Wipradnyadewi, Putu Ari Sayi Hatiningsih Shenni Maulina Suputra, I Gede Maha Adijaya Teguh Pribadi Girsang Teruo Sone Thobie E. B Kaban Tirmizhi Abubakar, Munkaila WAYAN REDI ARYANTA Wito Setioko Yanti Sinurat, Dame Yohanes Setiyo Yohanes Setiyo Yohannes Eko Putra Simanullang Yudisthira Dharma Bhusana Dasa Zainul Arifin