Claim Missing Document
Check
Articles

Found 3 Documents
Search
Journal : Makara Journal of Science

Detection of Submicroscopic Soil-Transmitted Helminth Infections from Fecal Samples in Nangapanda, Ende, Using Real-Time Polymerase Chain Reaction Maylasari, Roospita; Wulandhary, Sendy; Supali, Taniawati; Abinawanto, Abinawanto
Makara Journal of Science Vol. 18, No. 2
Publisher : UI Scholars Hub

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

Soil-transmitted helminth (STH) infections (Necator americanus (hookworm), Ancylostoma duodenale (hookworm), and Ascaris lumbricoides) can lead to anemia, malnutrition, and iron deficiency. Traditionally, STH infections have been diagnosed using microscopy to detect eggs in human fecal samples. However, there are several limitations of this method. The aim of this research was to detect the percentage of submicroscopic STH infections from human fecal samples (children, 5–18 years old) in Nangapanda, Ende, using the real-time polymerase chain reaction (PCR) method. The fecal samples were collected in two time periods, which were before and after treatment, using 400 mg of Albendazole. There were 242 samples in total, but only 45 negative samples from microscopic detection were tested with real-time PCR. The DNA samples were isolated and amplified wih primers of internal transcribed spacer (ITS-1 and ITS-2) region of rDNA. The detection of samples with real-time PCR generated an amplification curve in VIC, FAM, and Texas Red fluorophore. Three samples (6.7%) in pre-treatment were low load of DNA (N. americanus and A. lumbricoides) (Ct > 35). Four samples (9.1%) were low load of DNA (N. americanus) (Ct > 35) in post-treatment. Five samples (11.4%) were moderate load of DNA (A. lumbricoides) (30 < Ct < 35) in post-treatment. This study showed that real-time PCR could detect submicroscopic infections from specific species of hookworm and A. lumbricoides
Detection of Papua New Guinea Thalassemia Alpha Mutation in Gayo, Sumba, Ternate, and Timika Populations Nurfitriani, Risya; Abinawanto, Abinawanto; Noviyanti, Rintis; Trianti, Lely; Nainggolan, Ita M.
Makara Journal of Science Vol. 18, No. 2
Publisher : UI Scholars Hub

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

Papua New Guinea (PNG) mutation is a point mutation that occurs in noncoding region of alpha globin clusters. Polymorphism promotes an additional recognition site for transcription factor (GATA-1) which presumably downregulates alpha globin synthesis. The aim of this research is to detect PNG mutation in other populations in Indonesia, thus the results will be used for completing standard diagnoses in detecting alpha thalassemia mutation based on ethnic background. The method used in detecting PNG mutation was PCR-RFLP. Detection of 399 samples (MCH
Optimizing the Expression of Polyethylene Terephtalate Hydrolase-Encoding Synthetic Gene in Escherichia coli Arctic Express (DE3) Nataniel, Jocelyn; Ulfah, Maria; Achnafani, Dini; Nurhayati, Niknik; Sabbathini, Gabriela Christy; Wulandari, Sri Rezeki; Abinawanto, Abinawanto; Helianti, Is
Makara Journal of Science Vol. 28, No. 2
Publisher : UI Scholars Hub

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

The waste of polyethylene terephthalate (PET) plastic waste in Indonesia is a pressing concern due to its slow degradation and potential environmental damage. One promising solution is to utilize polyethylene terephthalate hydrolase from Ideonella sakaiensis (IsPETase), an enzyme that specifically degrades PET. However, inducing the expression of IsPETase synthetic gene in Escherichia coli BL21 (DE3) has been challenging because much of it remains insoluble. This study aimed to express IsPETase in E. coli Arctic Express (DE3) and optimize the conditions to enhance its production. First, pET22b(+)pelB-IsPETase was inserted into E. coli Arctic Express (DE3). The recombinant E. coli Arctic Express (DE3) was induced with isopropyl-β-D-1-thiogalactopyranoside (IPTG) and incubated at 10 °C. The fraction expressing soluble IsPETase was determined in different culture media, IPTG concentrations, induction times, and soni-cation durations. Parameters were optimized using a one-factor-at-a-time approach and then evaluated based on esterase specific activity and SDS-PAGE analysis. Results showed that IsPETase can be expressed in extracellular, periplasmic, and cytoplasmic soluble fractions. However, the extracellular fraction should be concentrated. Subsequent optimization focused only on the cytoplasmic fraction under optimal conditions, achieving a threefold increase in PETase specific activity compared with that under uninduced IPTG conditions. The reaction of PETase enzyme with PET and PCL was proven by weight loss, Scanning electron microscope (SEM), and Fourier transform infrared spectroscopy (FTIR). Although successful IsPETase expression and production optimization have been achieved, the specific activity remains low, prompting the need for ongoing expression optimization.
Co-Authors A. Sofyan A. Sofyan Abdul Basith Achmad Dinoto Achmad Dinoto Achnafani, Dini Ade Sunarma Agung Sudaryono Agus Haryadi Ahmad Aulia Jusuf Alimuddin Andi Salamah ANOM BOWOLAKSONO Arief Boediono ASRI SULFIANTI Bayu , Mariana D. Diki Nurul Huda Djamhuriyah S. Said DODDY IRAWAN SETYO UTOMO Dwiranti, Astari Endang C. Purba Endang Sukara Eni Kusrini Eni Kusrini Eni Kusrini Eni Kusrini, Eni Erma Primanita Hayuningtyas Fitrianingrum, Nisa Funahashi, Hiroaki H. Julendra Hidayat Hidayat Huriyah Adani Saoemi is helianti IS HELIANTI IS HELIANTI Isma Nur Azzizah Ita M. Nainggolan L. Istiqomah Lina Mulyawati Lulut Dwi Sulistyaningsih M. F. Karimy M. F. Karimy Maria Ulfah Maria Ulfah Mariana D. Bayu Marina Silalahi Marlina Ardiyani Maylasari, Roospita MILANI ANGGIANI Nataniel, Jocelyn NIKNIK NURHAYATI NIKNIK NURHAYATI Nisyawati Nova Anita Noviyanti, Rintis Nurfitriani, Risya Odang Carman Prakoso, Nurul Muhammad PUSPITA LISDIYANTI Putra Mahanaim Tampubolon Rabbil Pratama Aji Retno Lestari Retno Lestari Retno Lestari Retno Lestari Riska S. Wahyuningtyas Rita Rostika RONI RIDWAN Sabar Pambudi Sabbathini, Gabriela Christy Sanya Khaerunnisa Sawung Cindelaras, Sawung SHANNI FERNANDA Shanti Ratnakomala Siti Z Musthofa Solly Aryza Sulistiani ., Sulistiani Sulistiani Sulistiani Sulistiani Sulistiani, Sulistiani Sunarma , Ade Sundari, Ayu Mulia Taniawati Supali Trianti, Lely Uswatun Hasanah UTAMA ANDI Valerry Athalia Priyanka Wibowo Mangunwardoyo WIBOWO MANGUNWARDOYO Wulandari, Sri Rezeki Wulandhary, Sendy Yasman Yasman Yasman Yushinta Fujaya