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All Journal Natural Science: Journal of Science and Technology Jurnal Ilmu Lingkungan bionature Prosiding Seminar Biologi PROSIDING SEMINAR KIMIA Journal of Tropical Biodiversity and Biotechnology Indonesia Chimica Acta Indonesian Journal of Chemistry Indonesian Journal of Pure and Applied Chemistry Communications in Science and Technology Jurnal Ilmu Alam dan Lingkungan SELAPARANG: Jurnal Pengabdian Masyarakat Berkemajuan Chemistry Indonesian Journal of Chemical Research Scripta Biologica Fullerene Journal of Chemistry Indobiosains Molekul: Jurnal Ilmiah Kimia
Ahyar Ahmad
Universitas Hasanuddin
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Computer Science & IT Control & Systems Engineering Economics, Econometrics & Finance Education Engineering Environmental Science Health Professions Immunology & microbiology Languange, Linguistic, Communication & Media Law, Crime, Criminology & Criminal Justice Materials Science & Nanotechnology Medicine & Pharmacology Nursing Public Health Social Sciences Veterinary Other

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Journal : Molekul: Jurnal Ilmiah Kimia

 1 
Production, Characterization, and Toxicity Test of L-asparaginase from Vibrio alginolyticus Bacterial Symbiont of Green Algae Caulerpa lentillifera Kasturiasih, Ni Putu; Ahmad, Ahyar; Arfah, Rugaiyah A.; Khairunnur, Siti; Soekamto, Nunuk Hariani; Taba, Paulina; Hala, Yusafir; Karim, Harningsih
Molekul Vol 18 No 3 (2023)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20884/1.jm.2023.18.3.8153

Abstract

L-asparaginase is an enzyme that can be used as an anticancer therapeutic agent. This study aimed to optimize fermentation time for production, optimization, and to test the toxicity of L-asparaginase from Vibrio alginolyticus (V. alginolyticus) bacterial symbiont of green algae Caulerpa lentillifera (C. lentillifera). The activity of L-asparaginase enzyme assay and the toxicity test were done by using the Nessler method and the Brine Shrimp Lethality Test (BSLT) method respectively. The results show L-asparaginase with 66 hours of fermentation time indicates the highest enzyme activity. L-asparaginase mentioned has an optimum enzyme activity of 17.99 U/mL for 30 minutes of incubation time at 37 °C, and pH 7.5. The BSLT results show LC50 value of 17.83 μg/mL indicating the enzyme is bio-toxic with high-level toxicity, which can continue for cytotoxicity tests on cancer cells.
Chitinase Enzyme-Producing Endophytic Bacterias From the Roots of the Plant Gembolo (Dioscorea bulbifera): Isolation, Characterization and its Potential as an Antifungal Agent Yunita, Vivi Alfi; Natsir, Hasnah; Ahmad, Ahyar; Baharuddin, Maswati
Molekul Vol 19 No 1 (2024)
Publisher : Universitas Jenderal Soedirman

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.20884/1.jm.2024.19.1.9422

Abstract

Chitinase is an enzyme of the chitinolytic group that has many roles in agriculture, especially as an antifungal, because chitin is one of the constituent components of the fungal cell wall. This study aimed to isolate and identify endophytic bacteria from gembolo (Dioscorea bulbifera) roots and to characterize the chitinase enzyme from these endophytic bacteria to be used as an antifungal. Isolation and identification of gembolo plant root endophytic bacteria using PCR method of 16S rRNA gene amplification and sequencing. Characterization of the chitinase enzyme produced includes determining of optimum pH, temperature, and substrate UV-Vis spectrophotometer. Antagonistic test of the chitinase enzyme and endophytic bacterial isolates (isolate K4) Fusarium oxysporum. The results showed that bacterial isolate K4 had with chitinolytic index of 2.45 mm. Electrophoresis results with PCR 16s rRNA gene; the length of the amplified fragment is the position of 1300 bp. By doing the BLAST process in GenBank, the bacterial isolate has 97.93% similarity with Enterobacter cloacae. Then, this endophytic bacteria is called Enterobacter cloacae K4-G. This bacterium produced chitinase enzyme reaching maximum chitinase activity at the 38 hours with an activity of 0.0312 U/mL. The chitinase characterization results of E. cloacae K4-G showed that the optimum conditions were reached at at pH 6, temperature 45 ᵒC, and 2.5% substrate with a chitinase activity value of 0.2467 U/mL. Chitinase enzyme and bacteria Enterobacter cloacae K4-G can inhibit the growth of the fungus Fusarium oxysporum. Therefore, Chitinase from Enterobacter cloacae K4-G can be used as an antifungal pathogen in plants.
Co-Authors Abdul Karim Abdul Rauf Patong Abubakar, Andi Nur Fitriani Ade Rifka Junita Ahmad Fudhail  Majid Ajuk Sapar Alam, Muh. Nur Alfian Noor Ali Muhakim Andi Erwin Eka Putra Andi Evi Erviani Anita Anita Ardita R, Dian Fitrah Arfah, Rugaiyah A. Arfah, Rugaiyah Andi Arfiani Nur Aslinda, Wery Asmuddin Nasir Asmuddin Natsir Azis, Fitria Aziz, Fitria Burhanuddin Bahar Burhanuddinnur, Muhammad Cut Muthiadin dwyana, Zarsawaty Eva Johannes Fadliah, Fadliah Febryanti, Amalyah Firdaus Firdaus Firdaus Hamid Gita, Gita Hafsan, Hafsan Hanapi Usman Harningsih Karim Harningsih Karim Hasnah Natsir Indah Raya Irfandi, Rizal Isna Rasdianah Aziz Kasturiasih, Ni Putu Khairunnur, Siti Laily Agustina Laily Agustina, Laily M. Sabir Maming Gaffar, Maming Mardiyanti, Riska Mashuri Masri Maslan, Muhammad Maswati Baharuddin Miftahul Jannah Mochammad Hatta Muh. Yusri Karim Muhammad Nadir Muhammad Reza Primaguna Muhammad Zakir Munadi, Rachmin Negara, Satria Putra Jaya Nunuk H. Soekamto Nunuk Hariani Soekamto Nur Asmi Nur Indah Purnamasari Nur Umriani Nurfadini, Nurfadini Nurhikmah Nurhikmah Nurjannah Nurjannah Paulina Taba PRATAMA, IRHAM Putri, Tri Widayati Ramadani, Ananda Rasyid, Herlina Rauf, Wahyudin Ressy Dwiyanti Riksfardini Annisa ERMAWAR Risdianto, I Wayan Rosdiana Natzir Sappewali, Sappewali Sarlan, Sarlan SITI HALIMAH LAREKENG, SITI HALIMAH Sri Wahyuni Sukmawaty, Eka Sulistiani Jarre Suriati Eka Putri Syamsurya, Syamsurya USMAN - Usman Usman Yasser, M Yuniar Harviyanti Yunita, Vivi Alfi Yusafir Hala