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INDONESIA
Indonesian Journal of Biotechnology
Published by Universitas Gadjah Mada
ISSN : 08538654     EISSN : 20892241     DOI : -
Core Subject : Science,
Biochemistry, Genetics & Molecular Biology Immunology & microbiology Materials Science & Nanotechnology
The Indonesian Journal of Biotechnology (IJBiotech) is an open access, peer-reviewed, multidisciplinary journal dedicated to the publication of novel research in all aspects of biotechnology, with particular attention paid to the exploration and development of natural products derived from tropical—and especially Indonesian—biodiversity. IJBiotech is published biannually and accepts original research articles featuring well-designed studies with clearly analyzed and logically interpreted results. A strong preference is given to research that has the potential to make significant contributions to both the field of biotechnology and society in general.
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Articles 7 Documents
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Search results for , issue "Vol 28, No 4 (2023)" : 7 Documents clear
Cloning and characterization of bgl6111 gene encoding β‐glucosidase from bagasse metagenome Fitra Adi Prayogo; Benjarat Bunterngsook; Pattanop Kanokratana; Hermin Pancasakti Kusumaningrum; Dyah Wulandari; Anto Budiharjo
Indonesian Journal of Biotechnology Vol 28, No 4 (2023)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.81536

Abstract

β‐Glucosidase (BGL) is an essential enzyme for the hydrolysis of cellulose in industrial processes, but natural BGL enzymes are poorly understood. Metagenomics is a robust tool for bioprospecting in the search for novel enzymes from the entire community’s genomic DNA present in nature. The metagenomics approach simplifies the process of searching for new BGL enzymes by extracting DNA and retrieving its gene information through a series of bioinformatic analyses. In this study, we report the gene cloning, heterologous expression of the bgl6111 gene (accession number MW221260) in Pichia pastoris KM71, and the biochemical characterization of the recombinant enzyme. We successfully identified the bgl6111 sequence of 2,520 bp and 839 amino acids with a molecular size of 89.4 kDa. The amino acid sequence of the bgl6111 gene showed 67.61% similarity to BGL from an uncultured bacterium (ABB51613.1). The BGL product has the highest activity on the third day at 1.210 U/mL, categorized as low production. The enzymatic activity could enhance up to 539.8% of 7.742 U/mL by using the ultrafiltration method. Our findings provide insightful information that bgl6111 obtained from bagasse metagenome could be an alternative candidate for industrial applications in the future.
Chitosan Xylotrupes gideon encapsulated lemongrass leaf ethanol extract reduce H2O2‐induced oxidative stress in human dermal fibroblast Komariah Komariah; Pretty Trisfilha; Rahman Wahyudi; Nada Erica; Didi Nugroho; Yessy Ariesanti; Sarat Kumar Swain
Indonesian Journal of Biotechnology Vol 28, No 4 (2023)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.81544

Abstract

During phagocytosis, phagocyte cells discharge reactive oxygen species referred to as respiratory bursts, inducing a rise in pro‐oxidants and subjecting the cell to oxidative stress. Such stress is a biological mechanism related to an imbalance in pro‐oxidant/antioxidant homeostasis, which generates toxic reactive oxygen. Encapsulation is a coating process to improve the stability of bioactive compounds from lemongrass extract. Therefore, this study aims to determine the encapsulation activity of lemongrass leaf extract with chitosan X. gideon (LEChXg) to reduce the oxidative stress of fibroblasts. The research used the human dermal fibroblast (HDF) cell line, comprising negative and positive controls and use of LEChXg 100, 200, 300, 400, and 500 µg/mL. HDF cell migration was evaluated by employing the scratch wound healing method and the wound closure was oberseved at 0, 2, 4, 6, and 24 h intervals. The cell proliferation was observed at 24, 48, and 72 h using CCK‐8 at a 450 nm wavelength. The results showed that the observations at 0, 2, and 4 h did not demonstrate any significant difference on the cell migration (p > 0.05) among the groups. However, the wound closure at 4 and 6 h showed a significant difference (p < 0.05) with LEChXg 300 µg/mL. Despite the lack of any significant variation observed up to 24 h, fibroblast subjected to the stressor did not achieve complete closure. The groups treated with LEChXg were more stable in maintaining fibroblast proliferation up to the end of the observation than those with stressors at 24, 48, and 72 h. Fibroblast induced with a stressor was also more stable in maintaining migration and proliferation in groups receiving LEChXg 300 µg/mL.
A response surface methodology for the use of MIL‐101 as a catalyst for the one‐step synthesis of lactide Clara Novia; Catia Angli Curie; Misri Gozan
Indonesian Journal of Biotechnology Vol 28, No 4 (2023)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.82387

Abstract

Lactide is a vital monomer for producing high molecular weight polylactic acid (PLA) through ring‐opening polymerization. This study synthesized crude lactide from L‐lactic acid with MIL‐101 as the catalyst. MIL‐101 is a metal‐based catalyst with organic ligands (MOF) that was prepared by reacting Cr(NO3)3.9H2O with terephthalic acid (BDC). The formation of MIL‐101 was confirmed from Fourier‐transform infrared (FTIR) analysis. The role of MIL‐101 and the effect of temperature, time, and MIL‐101 loading, as well as their interactions in the conversion of lactic acid to crude lactide, were then investigated using the response surface method (RSM). Crude lactide was analyzed using 1H‐nuclear magnetic resonance (NMR) spectroscopy to confirm the presence of lactide. The RSM results indicated that the highest conversion of 22.84% can be obtained using a temperature of 175 °C, 1.5% w/w MIL‐101 loading, and a reaction time of 5 h. The RSM model showed that the interaction of MIL‐101 loading and reaction time strongly affected the conversion of lactic acid to lactide, with a P‐value of 0.0021 and an F‐value of 50.45. In contrast, the interaction of catalyst loading and temperature did not significantly affect the conversion of lactic acid to lactide, with a P‐value of 0.2565 and an F‐value of 1.75.
Thrombolytic protease characterization from leaves and fruit flesh of the jernang rattan plant (Daemonorops draco) Urbanus Yustus Lebuan; Roga Florida Kembaren; Merry Meryam Martgrita; Cut Rizlani Kholibrina
Indonesian Journal of Biotechnology Vol 28, No 4 (2023)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.82390

Abstract

Thrombolytic agents are used for thrombolytic therapy to dissolve blood clots that form in a blood vessel. All currently used thrombolytic agents have unfavorable shortcomings, such as gastrointestinal bleeding, allergic reactions, and thrombolytic agent resistance, treatment for some of which can be quite expensive. As a result, the search for thrombolytic agents derived from plants is currently taking place. Some plants have been discovered to contain protease enzymes with thrombolytic activity; pharmaceuticals derived from plants are believed to be safer. Jernang rattan (Daemonorops draco) is a plant of the Arecaceae family and is known to produce resin. Jernang rattan resin is also known to have antioxidant, antiseptic, antitumor, antimicrobial, and cytotoxic activity, but very limited information on proteolytic activity of the protease from this plant. This research aims to isolate proteases from the leaves and fruit flesh of the rattan jernang plant (D. draco) and to investigate the proteolytic activity of the isolated proteases. The protease was isolated from the leaves and the fruit flesh, and then partially purified by ammonium sulfate precipitation. The radial caseinolytic assay showed that protease in a 60% ammonium sulfate fraction gave a clear zone, with diameters of 1.4 cm and 1.8 cm for the protease isolated from leaves and fruit flesh, respectively. A Folin‐Ciocalteau assay showed that the enzymes isolated were able to hydrolyze casein and release L‐tyrosine, with activity of 0.158 U/mL and 0.174 U/mL for the protease from the leaves and fruit flesh, respectively. A fibrinogenolytic assay showed that the protease from the fruit flesh hydrolyzed the A‐α, B‐β and the γ chain of human fibrinogen, while the protease from the leaves hydrolyzed the A‐α and γ chain. Both proteases were inhibited by 56% by phenylmethylsulfonyl fluoride (PMSF), indicating that the enzymes are serine proteases. Based on the assay results obtained, it can be concluded that proteases isolated from the leaves and fruit flesh have potential as thrombolytic proteases.
Fermentation medium optimization of Streptomyces sp. as an antifungal agent against the Ganoderma boninensis pathogen in oil palm Syamsika Tahir; Widya Dwi Rukmi Putri; Agustin Krisna Wardani; Rofiq Sunaryanto
Indonesian Journal of Biotechnology Vol 28, No 4 (2023)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.82396

Abstract

Ganoderma boninensis is the most common fungus which attacks oil palm trees. However, a significant percentage of inhibition to the problem is found through the use of Streptomyces sp. The optimization of the Streptomyces sp. fermentation medium growth factors affects the secondary metabolites production. This study aimed to identify the best formulation of carbon and nitrogen sources and the optimum concentration of Streptomyces sp. fermentation medium for antifungal compound production. The results showed that the best sources of carbon and nitrogen were liquid glucose and monosodium glutamate in the inhibition zones of 16.7 mm and 6.3 mm, while the best concentration levels were 20 g/L and 14.19 g/L, respectively. The results of the first optimization showed an inhibition zone response and area (%) of the optimum high‐performance liquid chromatography (HPLC) chromatogram of 24.39 mm and 62.68 percent, respectively. Taking the suggestion of the first optimization, the second optimization produced 15.2 g/L and 8.3 g/L. The predicted value of the inhibition zone was 21.47 mm, and the area (%) of the HPLC chromatogram was 53.44 percent. The validation results showed an inhibition zone response of 22.01 mm and an HPLC chromatogram area (%) of 54.86 percent. The difference between the predicted and validation values was less than 5 percent; the validation value was thus in line with the value predicted by Design Expert 10.0.7. The chemical formula of the probable active compound is that of the cyclo(phenylalanyl‐prolyl) compound.
Kinetic modeling, optimization of biomass and astaxanthin production in Spirogyra sp. under nitrogen and phosphorus deficiency Nadia Delfi Zafira; Malvin Yulius Christian Pakpahan; I Putu Ikrar Satyadharma; Khairul Hadi Burhan; Erly Marwani
Indonesian Journal of Biotechnology Vol 28, No 4 (2023)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.82751

Abstract

This study studied the optimum nitrogen (N) and phosphorus (P) concentrations for biomass and astaxanthin production in Spirogyra sp. Spirogyra sp. was cultivated in Blue Green (BG) medium with N/P concentrations adjusted to 1.1/0.01; 1.1/0.03; 1.1/06; 1.1/0.09; 2.2/0.01; 2.2/0.03; 2.2/0.06; 2.2/0.09; 4.4/0.01; 4.4/0.03; 4.4/0.06; 4.4/0.09, 6.6/0.01; 6.6/0.03; 6.6/0.06 and 6.6/0.09 mM. The results showed an increase in biomass accumulation for lower concen‐ trations of N and N:P ratio with the highest accumulation at N/P 1.1/0.03 mM, i.e. 485 mgdryweight and a growth rate of 0.22 d‐1. Astaxanthin accumulation was also found to increase, with the highest at N/P 1.1/0.01 mM, i.e. 0.269 mg/gdryweight, on the 12th day of cultivation. Based on biomass and astaxanthin accumulation, the highest astaxanthin productivity was 0.07 μg/cm2/d at N/P concentration 1.1/0.09 mM. Kinetic models were developed using the Haldane and Luedeking–Piret equations. The growth and astaxanthin production parameters obtained were μmax 0.18±0.02 d‐1, kN 68.2 ± 24.2 mg/L, ki 301.8 ± 78.5 mg/L, YN 0.93 ± 0.68 gbiomass/nitrate, α 0.36 ± 0.69, β ‐0.01 ± 0.02, and kA 0.04 ± 0.03, thus indicating that a lower N concentration is suitable for the cultivation of Spirogyra sp. In conclusion, Spirogyra sp. should be cultivated under nitrogen deficiency for continuous astaxanthin production.
sgRNA design and in vitro nucleolytic analysis of the Cas9‐RNP complex for transgene‐free genome editing of the eIF4E1 gene from Capsicum an‐ nuum L. Josefanny Tham; Alfred Patisenah; Tommy Octavianus Soetrisno Tjia; Santiago Signorelli; Intan Taufik; Karlia Meitha
Indonesian Journal of Biotechnology Vol 28, No 4 (2023)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.86778

Abstract

Chili (Capsicum annuum L.) is a highly valued vegetable, renowned for its unique taste and aroma. However, chili production faces challenges in meeting the high demand due to infections caused by pathogens such as ChiVMV (potyvirus). Previous studies have suggested that chili eIF4E1 plays a crucial role in potyvirus gene transcription. Therefore, this study explores the potential of CRISPR‐Cas9‐based genome editing to enhance chili resistance by introducing premature stop codons or truncated proteins. Two sgRNAs were designed, targeting the first and second intron of the eIF4E1 gene. The production of Cas9 protein was assessed with varying IPTG concentrations in Escherichia coli BL21(DE3), carrying 4xNLS‐pMJ915v2‐sfGFP plasmid with a TEV protease cut‐site at the N terminal. The findings indicate that the optimal IPTG concentration is 500 µM. Purification using an IMAC column confirmed the presence of Cas9 in the initial 2 mL of the eluted fractions, as indicated by numerous background proteins. Nevertheless, successful formation of Cas9‐RNP complexes was achieved for both sgRNAs. The nucleolytic activity of Tag‐Cas9 (carrying the MBP‐tag) and Cas9 was confirmed through in vitro endonuclease activity assays. The next step involved transfecting chili protoplasts with these RNP complexes to edit the chili eIF4E1 gene.

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