Penurunan Salinitas Air Payau Menggunakan Filter Media Zeolit Teraktivasi dan Arang Aktif

Masalah utama dalam pengolahan air payau yakni tingkat salinitas yang tinggi. Zeolit dan arang aktif diketahui memiliki kemampuan yang baik dalam pengolahan air minum, sehingga penelitian ini menggunakan zeolit dan arang aktif sebagai media. Terdapat beberapa penelitian sebelumnya untuk menurunkan salinitas dan klorida pada air payau, penelitian yang menggunakan zeolit teraktivasi ammonium nitrat 2N dan surfaktan mampu menyisihkan klorida dan menurunkan salinitas untuk menghasilkan air minum yang memenuhi baku mutu, tetapi penelitian tersebut masih menggunakan sistem batch. Salah satu prinsip penyediaan air minum adalah kontinyuitas dimana air harus dapat memenuhi kebutuhan konsumen dalam waktu terus menerus secara kontinyu, sehingga penelitian ini menggunakan filter dengan sistem kontinyu untuk mengolah air payau. Penelitian dengan zeolit dan arang aktif sebagai media filter untuk menyisihkan klorida juga telah dilakukan sebelumnya, hasil penelitian tersebut belum dapat menghasilkan air yang sesuai dengan baku mutu air minum yakni klorida <250 mg/L dan salinitas <0,5 ppt. Sehingga pada penelitian ini, zeolit pada media filter diaktivasi dengan ammonium nitrat dan surfaktan untuk meningkatkan kemampuan penyisihannya. Penelitian ini dimulai dengan penelitian pendahuluan untuk mengetahui media terbaik pada filter yang mampu menurunkan klorida dan salinitas terbaik dari air payau yang dibuat secara artificial. Setelah didapatkan media paling baik kemudia diuji larutan aktivasi terbaik untuk meningkatkan efisiensi zeolit, dengan menggunakan aktivator ammonium nitrat dan surfaktan benzalkonium klorida. Penelitian utama dilakukan dengan variabel kecepatan 0,1 , 0,2 , 0,3, 0,03 m/jam, serta variasi konsentrasi klorida 1.000 mg/L, 5.000 mg/L dan 10.000 mg/L. Penelitian tambahan dilakukan menggunakan air sumur payau, untuk memberikan perbandingan kemampuan zeolit dalam menurunkan klorida dan salinitas pada air payau yang tidak artificial. Waktu breakthrough ditentukan berdasarkan perhitungan menggunakan pendekatan kinetika adsorpsi. Hasil penelitian menunjukkan zeolit teraktivasi surfaktan benzalkonium klorida dengan kecepatan filtrasi 0,03 m/jam merupakan yang paling baik dalam menyisihkan klorida dan menurunkan salinitas, dengan nilai rata-rata penyisihan klorida pada konsentrasi 10.000 mg/L adalah 20,66% dan konsentrasi 5.000 mg/L adalah 26,77%, serta konsentrasi 1.000 mg/L adalah 38,59%. Penurunan salinitas pada konsentrasi 10.000 mg/L adalah 15,55%, dan pada konsentrasi 5.000 mg/L adalah 16,51%, pada konsentrasi 1.000 mg/L adalah 20,94%. Hasil perhitungan waktu breakthrough pada konsentrasi 10.000 mg/L, kecepatan 0,3 m/jam 5,5 hari, kecepatan 0,2 m/jam 4,8 hari, kecepatan 0,1 m/jam 3,3 hari, kecepatan 0,03 m/jam 3,69 hari. Pada konsentrasi 5.000 mg/L, kecepatan 0,3 m/jam 3,4 hari, kecepatan 0,2 m/jam 3,73 hari, kecepatan 0,1 m/jam 3,29 hari, kecepatan 0,03 m/jam 3,03 hari.Pada konsentrasi 1.000 mg/L, kecepatan 0,3 m/jam 6,7 hari, kecepatan 0,2 m/jam 10,72 hari, kecepatan 0,1 m/jam 13,8 hari, kecepatan 0,03 m/jam 24,5 hari. ======================================================== ============= The main problem in brackish water treatment is the high salinity level. Zeolite and activated carbon are known to have a good ability in water treatment process, therefore this research used zeolite and activated carbon as the media. There were several previous research to reduce salinity and remove chlorida in brackish water, the research used zeolite activated by ammonium nitrate 2N and surfactant for brackish water treatment process, but the reaserch still used batch system. One of water supply principle is continuity, which is mean water must able to meet the consumen need continuesly. Therefore this research used filter with continuous system. The research using zeolite and activated carbon as filter media to remove chlorida also have been done before, but the research results had not been able to produce water that meet quality standart for drinking water which is <250 mg/L for chlorida and <0,5 ppt for salinity. This research aim to improve filter ability in producing drinking water by using ammonium nitrat and surfactant for zeolite activation. This research begun with a preliminary study to find out the best media in removing chloride and salinity of artificial brackish water. After that, activator was tested to determine the best activation in improving zeolite efficiency removal, using ammonium nitrate and benzalkonium chloride surfactant as activator. The main research conducted with variable velocities of 0,1, 0,2, 0,3 , 0,03 m/h and variations in chloride concentrations of 1.000 mg/L, 5.000 mg / L and 10.000 mg / L. The additional reasearch used brackish ground water to provide comparison of filter ability in removing chlorida and salinity in a non artificial water. The breakthrough time determined by adsorption kinetic approach. The result of this research show zeolite activated by surfactant benzalkonium chlorida with filtration rate 0,03 m/hour give the best performace in removing chloride. The average of chloride removal in concentration of 10.000 mg/L is 20,66% in concentration 5.000 mg/L is 26,77%, in concentration 1.000 mg/L is 38,59%. Salinity reduction in concentration 10.000 mg/L is 15,55%, in concentration 5.000 mg/L is 16,51%, and in concentration 1.000 mg/L is 20,94%. The result of breakthrough time in chloride concentration 10.000 mg/L, in filtration rate 0,3 m/h is 5,5 days, in filtration rate 0,2 m/h is 4,8 days, in filtration rate 0,1 m/h is 3,3 days, in filtration rate 0,03 m/h is 3,69 days. The chloride concentration 5.000 mg/L, in filtration rate 0,3 m/h is 3,4 days, in filtration rate 0,2 m/h is 3,73 days, in filtration rate 0,1 m/h is 3,29 days, in filtration rate 0,03 m/h is 3,03 days The chloride concentration 1.000 mg/L, in filtration rate 0,3 m/h is 6,7 days, in filtration rate 0,2 m/h is 10,72 days, in filtration rate 0,1 m/h is 13,8 days, in filtration rate 0,03 m/h is 24,5 days

The Joint Council on Thoracic Surgery Education (JCTSE) “Educate the Educators” Faculty Development Course: Analysis of the First 5 Years

BACKGROUND: Since 2010, the Joint Council on Thoracic Surgery Education, Inc (JCTSE) has sponsored an annual "Educate the Educators" (EtE) course. The goal is to provide United States academic cardiothoracic surgeons (CTS) the fundamentals of teaching skills, educational curriculum development, and using education for academic advancement. This report describes the course development and evaluation along with attendee's self-assessment of skills through the first 5 years of the program. METHODS: The content of this 2½-day course was based on needs assessment surveys of CTS and residents attending annual meetings in 2009. From 2010 to 2014, EtE was offered to all CTS at training programs approved by the Accreditation Council for Graduate Medical Education. Course content was evaluated by using end-of-course evaluation forms. A 5-point Likert scale (1 = poor, 5 = excellent) was used to obtain composite assessment mean scores for the 5 years on course variables, session presentations, and self-assessments. RESULTS: With 963 known academic CTS in the United States, 156 (16.3%) have attended, representing 70 of 72 training programs (97%), and 1 international surgeon attended. There were also 7 program coordinators. Ratings of core course contents ranged from 4.4 to 4.8, accompanied with highly complementary comments. Through self-assessment, skills and knowledge in all content areas statistically improved significantly. The effect of the course was evaluated with a follow-up survey in which responders rated the program 4.3 on the usefulness of the information for their career and 3.9 for educational productivity. CONCLUSIONS: The EtE program offers an excellent opportunity for academic CTS to enhance their teaching skills, develop educational activities, and prepare for academic promotion. With its unique networking and mentorship environment, the EtE program is an important resource in the evolution of cardiothoracic surgical training in the United States

A non-canonical scaffold-type E3 ligase complex mediates protein UFMylation

Protein UFMylation, i.e., post‐translational modification with ubiquitin‐fold modifier 1 (UFM1), is essential for cellular and endoplasmic reticulum homeostasis. Despite its biological importance, we have a poor understanding of how UFM1 is conjugated onto substrates. Here, we use a rebuilding approach to define the minimal requirements of protein UFMylation. We find that the reported cognate E3 ligase UFL1 is inactive on its own and instead requires the adaptor protein UFBP1 to form an active E3 ligase complex. Structure predictions suggest the UFL1/UFBP1 complex to be made up of winged helix (WH) domain repeats. We show that UFL1/UFBP1 utilizes a scaffold‐type E3 ligase mechanism that activates the UFM1‐conjugating E2 enzyme, UFC1, for aminolysis. Further, we characterize a second adaptor protein CDK5RAP3 that binds to and forms an integral part of the ligase complex. Unexpectedly, we find that CDK5RAP3 inhibits UFL1/UFBP1 ligase activity in vitro. Results from reconstituting ribosome UFMylation suggest that CDK5RAP3 functions as a substrate adaptor that directs UFMylation to the ribosomal protein RPL26. In summary, our reconstitution approach reveals the biochemical basis of UFMylation and regulatory principles of this atypical E3 ligase complex

RavN is a member of a previously unrecognized group of Legionella pneumophila E3 ubiquitin ligases

The eukaryotic ubiquitylation machinery catalyzes the covalent attachment of the small protein modifier ubiquitin to cellular target proteins in order to alter their fate. Microbial pathogens exploit this post-translational modification process by encoding molecular mimics of E3 ubiquitin ligases, eukaryotic enzymes that catalyze the final step in the ubiquitylation cascade. Here, we show that the Legionella pneumophila effector protein RavN belongs to a growing class of bacterial proteins that mimic host cell E3 ligases to exploit the ubiquitylation pathway. The E3 ligase activity of RavN was located within its N-terminal region and was dependent upon interaction with a defined subset of E2 ubiquitin-conjugating enzymes. The crystal structure of the N-terminal region of RavN revealed a U-box-like motif that was only remotely similar to other U-box domains, indicating that RavN is an E3 ligase relic that has undergone significant evolutionary alteration. Substitution of residues within the predicted E2 binding interface rendered RavN inactive, indicating that, despite significant structural changes, the mode of E2 recognition has remained conserved. Using hidden Markov model-based secondary structure analyses, we identified and experimentally validated four additional L. pneumophila effectors that were not previously recognized to possess E3 ligase activity, including Lpg2452/SdcB, a new paralog of SidC. Our study provides strong evidence that L. pneumophila is dedicating a considerable fraction of its effector arsenal to the manipulation of the host ubiquitylation pathway.Funding: This work was funded by the Intramural Research Program of the National Institutes of Health (to MPM)(Project Number: 1ZIAHD008893-07) and by the Spanish Ministry of Economy and Competitiveness Grant (to AH)(BFU2014-59759-R) and the Severo Ochoa Excellence Accreditation (to AH)(SEV-2016-0644). This study made use of the Diamond Light Source beamline I04 (Oxfordshire, UK) and ALBA synchrotron beamline BL13-XALOC, funded in part by the Horizon 2020 programme of the European Union, iNEXT (H2020 Grant # 653706). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript

Identifying and Validating Tankyrase Binders and Substrates: A Candidate Approach.

The poly(ADP-ribose)polymerase (PARP) enzyme tankyrase (TNKS/ARTD5, TNKS2/ARTD6) uses its ankyrin repeat clusters (ARCs) to recognize degenerate peptide motifs in a wide range of proteins, thereby recruiting such proteins and their complexes for scaffolding and/or poly(ADP-ribosyl)ation. Here, we provide guidance for predicting putative tankyrase-binding motifs, based on the previously delineated peptide sequence rules and existing structural information. We present a general method for the expression and purification of tankyrase ARCs from Escherichia coli and outline a fluorescence polarization assay to quantitatively assess direct ARC-TBM peptide interactions. We provide a basic protocol for evaluating binding and poly(ADP-ribosyl)ation of full-length candidate interacting proteins by full-length tankyrase in mammalian cells