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All Journal Biota INDONESIAN JOURNAL OF MEDICAL LABORATORY SCIENCE AND TECHNOLOGY Journal of Multidisciplinary Applied Natural Science
Siti Soleha
Biology Department, Faculty Of Science And Technology, Universitas Islam Negeri Raden Fatah Palembang, Palembang, South Sumatera, Indonesia.
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Energy Environmental Science Health Professions Immunology & microbiology Materials Science & Nanotechnology Mathematics Medicine & Pharmacology Physics Social Sciences

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Aktivitas Enzimatis Eko-Enzim Averrhoa bilimbi L. Di Kabupaten Plaju Sumatera Selatan Dengan Variasi pH Siti Soleha; Delima Engga maretha; Andi Saputra; Siti Rachmi Indahsari; Binsar Butar Butar; Ahma Adi Suhendra; Maharani Maharani; Harlis Harlis; Hari Kapli
Biota Vol 9 No 2 (2023): Jurnal Biota 2023
Publisher : Faculty of Science and Technology Universitas Islam Negeri Raden Fatah Palembang

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.19109/Biota.v9i2.16460

Abstract

Enzymes are biocatalysts that have many benefits in the industry and the environment. Eco-enzymes are reported to have amylase, lipase, and protease activities. Enzymatic activity is strongly influenced by several factors, one of which is pH. This study aims to determine the optimum enzymatic activity (amylase, lipase and protease) of Averrhoa bilimbi L. fruit eco-enzymes with various pH treatments (5, 6, 7, 8). Enzymatic activity was measured using a spectrophotometric method. Amylase activity assay using starch as a substrate. Casein and para nitrophenol palmitate were used as substrates. Casein was used as a substrate in the protease activity assays. In the lipase activity assays, para nitrophenol palmitate was used as substrate. Data analysis results are presented in graphical and descriptive. Averrhoa bilimbi L. fruit eco-enzyme has a protein concentration of 0.459 mg/ml. The optimum activity of amylase at pH 5 was 11,713.871 U/mg. Optimum activity and protease activity occurred at pH 8 and 6 of 3.667 U/mg and 13,400.77 U/mg, respectively.
Potential of Eco-enzyme Averrhoa bilimbi L. Fruit as an Innovation in Tempeh Wastewater Treatment in Plaju District, South Sumatra Siti Soleha; Delima Engga Maretha; Andi Saputra
Journal of Multidisciplinary Applied Natural Science Vol. 5 No. 1 (2025): Journal of Multidisciplinary Applied Natural Science
Publisher : Pandawa Institute

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.47352/jmans.2774-3047.224

Abstract

Tempeh home industries have been established in residential areas, one of which is in the assisted village of PT Pertamina Internasional RU III Plaju Factory, Palembang, South Sumatra. Eco-enzyme is one of the methods for processing and reducing pollutant organic matter in liquid waste. This study aims to determine the eco-enzyme characteristics of Averrhoa bilimbi L. fruit and exploit its potential to reduce chemical oxygen demand (COD), total suspended solid (TSS), and total dissolved solid (TDS) in tempeh wastewater. Eco-enzymes are characterized by measuring pH, COD, TSS, TDS, and most probable number (MPN). The reduction in COD, TSS and TDS of tempeh wastewater was observed using a simple bioreactor which was treated with the addition of 10% eco-enzyme (three replicates) and without the addition of eco-enzyme (control). The characterization results showed that the eco-enzyme of A. bilimbi L. fruit had a pH of 1.84, COD of 85.33 mg/L, TSS of 440 mg/L, TDS of 15,800 mg/L, protein concentration of 0.459 U/mg, and MPN value of 0.03 CFU/100 mL. The COD value of tempeh liquid waste can be reduced from the initial COD of 256 to 154.67 mg/L. The TSS value of tempeh wastewater decreased by 60% from the initial value of 4,000 mg/L. It takes 18 days to reduce the TSS content below the quality standard. The TDS value of tempeh liquid waste can be reduced by 70% from the initial TDS of 7,333.33 to 1,666.67 mg/L.
Molecular approach to the characterization of lipase encoding genes from Moraxella sp. SBE01 Siti Soleha; Syarifah Syarifah; Tito Nurseha; Awalul Fatiqin; Endah Retnaningrum; Yitro Serang
JURNAL INDONESIA DARI ILMU LABORATORIUM MEDIS DAN TEKNOLOGI Vol 6 No 2 (2024): Promising and Valuable Research Towards Diagnosis, Prognosis and Treatment of Dis
Publisher : Universitas Nahdlatul Ulama Surabaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.33086/ijmlst.v6i2.5596

Abstract

Lipase from Moraxella sp. SBE01 is an expression of the gene encoding lipase. Detection and characterization of the Moraxella sp. SBE01 lipase coding gene is necessary for large-scale lipase production through genetic engineering. This study aimed to observe the molecular weight, amino acid sequence, length, and conserved amino acids in the DNA encoding the lipase gene, with the goal of identifying and characterizing the lipase-coding gene from Moraxella sp. SBE01. The primer design process was conducted to amplify the lipase gene from Moraxella sp. SBE01 using specialized software for sequence alignment and phylogenetic analysis. Amplification was carried out using PCR with the designed primer, forward primer (GTC ATG ATG TAC TTC CAY GGN GGN GG), reverse primer (GGT TGC CGC CGG CDS WRT CNC C). PCR was carried out under pre-denatured conditions at 95°C (3 minutes), followed by 30 cycles of denaturation at 95°C, annealing at 66°C (30 seconds), 70°C elongations (1 minute) and final elongation of 70°C (10 minutes). The PCR results were electrophoresed using 1% agarose gel with a 1 kb DNA marker. The PCR results were sequenced and analyzed for gene and amino acid sequences and the type of lipase expressed. Sequencing resulted in 387 bp of the nucleotide sequence. The gene and amino acid sequences from Moraxella sp. SBE01 had high homology with the gene and amino acid sequences from Moraxella sp. strain TA144. The lipase gene encodes a protein consisting of 129 amino acids and contains a conserved HGG (His-Gly-Gly) motif, which is characteristic of lipases in family IV, also known as the hormone-sensitive lipase (HSL) family. This conserved sequence suggests that the lipase shares structural and functional similarities with other enzymes in the HSL family, playing a key role in lipid metabolism.
Co-Authors Ahma Adi Suhendra Andi Saputra Andi Saputra Binsar Butar Butar Delima Engga Maretha Delima Engga maretha Endah Retnaningrum Fatiqin, Awalul Hari Kapli Harlis Harlis Maharani Maharani Siti Rachmi Indahsari Syarifah Syarifah Tito Nurseha Yitro Serang