C. PENURUNAN KADAR LOGAM BERAT LIMBAH CAIR INDUSTRI EMAS DENGAN KAUSTIK SODA

2018 ◽  
Vol 1 (2) ◽  
pp. 16-29
Author(s):  
Agung Rasmito ◽  
Suhadi .
Keyword(s):  
Ph Optimum

Penelitian ini bertujuan untuk menurunkan kadar logam berat pada limbah cair  industri emas (PT X)  di Surabaya. Limbah industri PT. X ini memiliki kandungan logam – logam berat yang dapat disetarakan dengan limbah industri Electroplating. Limbah cair dari industri perhiasan emas sebagian besar merupakan limbah anorganik dengan kandungan asam yang cukup tinggi (pH rendah). Metode yang digunakan adalah metode presipitasi(pengendapan) dengaan beberapa variable yaitu jenis bahan pengendap(NaOH dan CaOH), pH larutan dan waktu pengendapan. Dari hasil penelitian diketahui bahwa , dengan penambahan Ca(OH) maupun NaOH semakin tingi pH , maka semakin besar pula % Removal logam Cu, Ni, Zn dan Fe. Demikian pula  dengan variable waktu flokulasi maka semakin lama waktu flokulasi maka semakin besa.% Removal logam Cu, Ni, Zn dan Fe. Untuk pH optimum yang  dapat menurunkan kadar logam Cu, Ni, Zn dan Fe adalah pada pH 12. Besarnya % removal logam Cu, Ni, Zn & Fe dengan penambahan koagulan NaOH berturut – turut adalah 99.993% , 99.877%, 99.946% dan 99.935%. Besarnya % removal logam Cu, Ni, Zn dan Fe dengan penambahan koagulan Ca(OH)2 berturut – turut adalah 99.994%, 99.936%, 99.949% dan 99.941%. Sedangkan waktu flokulasi optimum untuk menurunkan kadar logam Cu, Ni, Zn dan Fe adalah pada waktu flokulasi 30 menit.

The Uptake of Adenine by Isolated Human Platelet Membranes

1974 ◽  
Vol 32 (02/03) ◽  
pp. 457-464
Author(s):  
Paul C. French ◽  
Jan J. Sixma ◽  
Holm Holmsen
Keyword(s):  
Human Platelet ◽  
Facilitated Diffusion ◽  
Adenine Phosphoribosyltransferase ◽  
Ph Optimum ◽  
Intact Cells ◽  
Platelet Membranes ◽  
Group Translocation ◽  
Triton X

SummaryAdenine uptake into isolated platelet membranes had about the same Km (151 ± 21 • 9 nM) as uptake into intact cells (159 ± 21 nM) and was also competitively inhibited by papaverine and hypoxanthine. No uptake occurred at 0° and accumulated adenine was converted to AMP. AMP was not firmly bound to protein as judged by chromatography of triton X-100 solubilized membranes on Sephadex G25. The pH optimum for adenine uptake was at pH 5-5. Exogenous 5-phosphoribosyl-l-pyrophos- phate strongly stimulated uptake. These data may be explained by uptake of adenine by facilitated diffusion followed by conversion to AMP by adenine phosphoribosyltransferase but group translocation cannot be entirely excluded.

Isolation and Characterization of Plasminogen Activator from Pig Leucocytes

1974 ◽  
Vol 31 (01) ◽  
pp. 072-085 ◽  
Author(s):  
M Kopitar ◽  
M Stegnar ◽  
B Accetto ◽  
D Lebez
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Ph Optimum ◽  
Isolation And Characterization ◽  
Ph Range ◽  
Inhibition Studies ◽  
Final Purification

SummaryPlasminogen activator was isolated from disrupted pig leucocytes by the aid of DEAE chromatography, gel filtration on Sephadex G-100 and final purification on CM cellulose, or by preparative gel electrophoresis.Isolated plasminogen activator corresponds No. 3 band of the starting sample of leucocyte cells (that is composed from 10 gel electrophoretic bands).pH optimum was found to be in pH range 8.0–8.5 and the highest pH stability is between pH range 5.0–8.0.Inhibition studies of isolated plasminogen activator were performed with EACA, AMCHA, PAMBA and Trasylol, using Anson and Astrup method. By Astrup method 100% inhibition was found with EACA and Trasylol and 30% with AMCHA. PAMBA gave 60% inhibition already at concentration 10–3 M/ml. Molecular weight of plasminogen activator was determined by gel filtration on Sephadex G-100. The value obtained from 4 different samples was found to be 28000–30500.

Efektivitas Biokoagulan Cangkang Telur Ayam Ras dan Kulit Pisang Kepok (Musa Balbisiana ABB) dalam Menurunkan Turbiditas, TDS, dan TSS dari Limbah Cair Industri Farmasi

al-Kimiya ◽  
2020 ◽  
Vol 7 (1) ◽  
pp. 47-54
Author(s):  
Hesty Nuur Hanifah ◽  
Ginayanti Hadisoebroto ◽  
Turyati Turyati ◽  
Ineu Sintia Anggraeni
Keyword(s):  
Total Suspended Solid ◽  
Suspended Solid ◽  
Ph Optimum ◽  
Musa Balbisiana

Koagulasi merupakan tahap awal dalam proses pengolahan limbah cair. Salah satu industri yang berpotensi untuk menimbulkan pencemaran air bila limbah cairnya tidak dikelola dengan baik adalah industri farmasi. Cangkang telur ayam ras dan kulit pisang kepok merupakan limbah padat yang belum termanfaatkan, padahal kedua bahan tersebut mengandung zat-zat yang bisa membantu dalam proses koagulasi. Oleh karena itu, peneliti tertarik untuk mengembangkan biokoagulan dari cangkang telur ayam ras dan kulit pisang kepok. Penelitian ini bertujuan untuk mengetahui efektivitas dari cangkang telur ayam ras dan kulit pisang kepok sebagai biokoagulan dalam menurunkan nilai turbiditas, TDS (Total Disolved Solid) dan TSS (Total Suspended Solid) dari limbah cair industri farmasi. Alat yang digunakan dalam penelitian ini adalah jartest. Sampel air limbah yang digunakan dalam percobaan ini yaitu sampel air limbah industri farmasi dari PT Sinkona Indonesia Lestari. Berdasarkan hasil penelitian  menunjukkan bahwa biokoagulan cangkang telur ayam mempunyai dosis optimum yaitu 50 g/500 mL dan pada pH optimum 8 terjadi penurunan turbiditas sebesar 81,18%, TDS sebesar 24,3% dan TSS sebesar 82,05%. Sedangkan  biokoagulan kulit pisang kepok mempunyai dosis optimum 5 g/500 ml dan pada pH optimum 2 terjadi penurunan  turbiditas sebesar   94,9%, TDS 51,3% dan TSS  83,2%. Dari data tersebut bisa disimpulkan bahwa cangkang telur ayam ras dan kulit pisang kepok bisa dimanfaatkan sebagai biokoagulan untuk pengolahan limbah cair dari industri farmasi.

FERMENTATIVE HYDROLYTIC PREPARATION METHODS OF CEREAL WORT FOR ALCOHOL FERMENTATION

1970 ◽  
pp. 52-56
Author(s):  
Е. M. Serba ◽  
М. B. Overchenko ◽  
L. V. Rimareva ◽  
N. I. Ignatova ◽  
А. E. Orekhova ◽  
...  
Keyword(s):  
Alcoholic Fermentation ◽  
Raw Materials ◽  
Alcohol Concentration ◽  
Activity Level ◽  
Optimal Dosage ◽  
Main Role ◽  
Alcohol Fermentation ◽  
Ph Optimum ◽  
Amylolytic Enzyme ◽  
Enzyme Preparations

In the production of alcohol in the preparation of grain raw materials for fermentation, the main role is given to enzyme preparations of amylolytic action, which are key enzymes that catalyze the hydrolysis of starch. Amylolytic enzyme preparations with a different composition of enzymes and their level of activity, a mechanism of biocatalytic effect on starch, and a range of thermal and pH optimum are widely represented on the Russian market. The development of optimal conditions for the preparation of grain wort, the rational selection and dosage of concentrated enzyme preparations, the properties of which correspond to the parameters of the technological process, will ensure the effective preparation of starch for fermentation, and increase the profitability of alcohol production. The aim of this work was to study the influence of enzyme preparations of amylolytic action and the conditions of their use on the efficiency of the process of alcoholic fermentation and the yield of the final product, ethanol. The effect of various dosages of enzyme preparations of glucoamylase action, with a different ratio of the main enzyme glucoamylase and minor enzyme α-amylase, as well as methods for preparing wheat wort on the process of alcoholic fermentation, was studied. It was found that the enzyme preparation, the source of glucoamylase, in which α-amylase was present in a ratio of 15: 1 (in terms of activity level), turned out to be more effective in fermenting prepared wheat wort: its optimal dosage was 8 units. GLS / g starch. The presence of a sufficient amount of α-amylase in this preparation compensated for the dosage of thermostable α-amylase. The alcohol concentration in the mash was 10.2% vol., The alcohol yield was 67.9 cm3 / 100 g of starch. When glucoamylase with a lower ratio of the main and minor enzyme (75: 1) was used at the saccharification stage, an increase in the wort fermentation depth was observed with an increase in the concentration of glucoamylase to 9-10 units of GLS / g and α-amylase to 0.5 units. AC / g. It was also found that an increase in the duration of enzymatic-hydrolytic preparation of the wort had a positive effect on the fermentation process, the alcohol concentration in the mash increased to 10.2 vol.%. It was shown that the introduction of proteases into the wort helps to reduce the viscosity of grain wort, enriching it with assimilable yeast amino acids, which leads to an increase in the yield of alcohol. It has been confirmed that the synergy of the action of enzymes of amylolytic and proteolytic effects on polymers of grain raw materials allows to increase the efficiency of their conversion to ethanol. The conditions of enzymatic-hydrolytic processing of grain raw materials for fermentation are developed. The use of the digestion stage did not significantly affect the fermentation results of wheat wort.

PEMBUATAN DAN KARAKTERISASI SERAT HOLLOW DARI SELULOSA BAKTERIAL DENGAN NANOPARTIKEL ZnO UNTUK PENGOLAHAN AIR LIMBAH TEKSTIL

Arena Tekstil ◽  
2014 ◽  
Vol 29 (1) ◽  
Author(s):  
Rizka Yulina ◽  
Srie Gustiani ◽  
Wulan Septiani
Keyword(s):  
Fourier Transform ◽  
Acetobacter Xylinum ◽  
Wet Spinning ◽  
Ph Optimum ◽  
Infra Red ◽  
Remazol Black

Selulosa bakterial mempunyai sifat mekanik yang baik untuk digunakan sebagai membran pada proses pengolahan air limbah tekstil. Pada penelitian ini dilakukan pembuatan dan karakterisasi serat hollow dari bahan baku selulosa bakterial nata de coco dengan penambahan nanopartikel ZnO sebagai fotokatalis terimmobilisasi. Selulosa bakterial disintesis menggunakan bakteri Acetobacter xylinum di dalam medium air kelapa dan gula. Selulosa bakterial dilarutkan bersama dengan nanopartikel ZnO menggunakan pelarut cuprietilen diamina (Cuen) dengan variasi selulosa bakterial 2,25% dan 2,50%. Serat berbentuk hollow dihasilkan dari proses wet spinning menggunakan koagulan NaOH. Serat hollow yang telah melalui koagulan kemudian direndam dalam larutan asam, gliserol, dan alkohol, dengan variasi waktu perendaman asam selama 1 dan 2 hari. Uji kekuatan tarik menunjukkan hasil yang terbaik yakni sebesar 815,72 gf pada konsentrasi selulosa bakterial 2,50% dan perendaman asam selama 2 hari. Dari hasil uji gugus fungsi menggunakan spektroskopi Fourier Transform Infra Red (FTIR), terdapat beberapa gugus fungsi yang menunjukkan keberadaan selulosa dan nanopartikel ZnO. Proses dekolorisasi fotokatalitik terhadap air limbah tekstil artifisial yang mengandung zat warna reaktif Remazol Black 5 (RB5) menunjukkan bahwa pH optimum proses penyisihan warna yakni pada pH 9 dan dihasilkan persen penyisihan warna yang tertinggi yaitu 90,32%. Pada kondisi yang sama, proses dekolorisasi RB5 menggunakan serat hollow tanpa nanopatikel ZnO hanya menghasilkan persen penyisihan warna sebesar 32,10%. Berdasarkan laju penyisihan zat warna, aktivitas degradasi fotokatalitik terbesar (k’ = 0,2615) diperoleh pada konsentrasi ZnO 10% dan konsentrasi zat warna RB5 10 ppm.

Polarographic study of hydrolysis of [8-lysine]vasopressin and its derivatives with blood serum of pregnant women

1980 ◽  
Vol 45 (4) ◽  
pp. 1099-1108 ◽  
Author(s):  
Mikuláš Chavko ◽  
Michal Bartík ◽  
Evžen Kasafírek
Keyword(s):  
Blood Serum ◽  
Pregnant Women ◽  
Degree Of Hydrolysis ◽  
Polarographic Study ◽  
Ph Optimum ◽  
Lysine Vasopressin ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of ◽  
Vasopressin Analogues

A polarographic study of the hydrolysis of [8-lysine]vasopressin and some hormonogens of the vasopressin series with the blood serum of women in the last week of pregnancy was studied. The dependence of hydrolysis on pH (pH optimum: 7.4-7.50, substrate concentration (Km 1.2 . 10-5M), pH stability and thermal stability were determined. The rate of hydrolysis of individual vasopressin analogues decreases in the order: [8-lysine]vasopressin > Nα-glycyl-prolyl[8-lysine]-vasopressin > Nα-leucyl-[8-lysine]vasopressin > Nα-alanyl-[8-lysine]vasopressin > Nα-phenyl alanyl-[8-lysine]vasopressin > Nα-diglycyl-[8-lysine]vasopressin > Nα-prolyl-[8-lysine]vasopressin > Nα-triglycyl-[8-lysine]vasopressin > Nα-sarcosyl-glycyl-[8-lysine]vasopressin. The degree of hydrolysis gradually increases to a multiple with the length of the pregnancy in consequence of the presence of oxytocine. However, vasopressin is also hydrolysed to a small extent with the enzymes from the blood sera of non-pregnant women. Under similar analytical conditions oxytocin was not hydrolysed with the sera of non-pregnant women and therefore oxytocin is a more suitable substrate than vasopressin for polarographic determination of serum oxytocinase.

Purine nucleoside phosphorylase: Isolation and characterization

1990 ◽  
Vol 55 (12) ◽  
pp. 2987-2999 ◽  
Author(s):  
Katarina Šedivá ◽  
Ivan Votruba ◽  
Antonín Holý ◽  
Ivan Rosenberg
Keyword(s):  
Molecular Weight ◽  
Purine Nucleoside Phosphorylase ◽  
Purine Nucleoside ◽  
Leukemia Cells ◽  
Ph Optimum ◽  
Nucleoside Phosphorylase ◽  
Isolation And Characterization ◽  
Reaction Proceeds ◽  
The Matrix ◽  
Sepharose 4B

Purine nucleoside phosphorylase (PNP) from mouse leukemia cells L1210 was purified to homogeneity by a combination of ion exchange and affinity chromatography using AE-Sepharose 4B and 9-(p-succinylaminobenzyl)hypoxanthine as the matrix and the ligand, respectively. The native enzyme has a molecular weight of 104 000 and consists of three subunits of equal molecular weight of 34 000. The results of isoelectric focusing showed that the enzyme is considerably microheterogeneous over the pI-range 4.0-5.8 and most likely consists of eight isozymes. The temperature and pH-optimum of phosphorolysis, purine nucleoside synthesis and also of transribosylation is identical, namely 55 °C and pH 7.4. The transribosylation reaction proceeds in the presence of phosphate only. The following Km-values (μmol l-1) were determined for phosphorolysis: inosine 40, 2'-deoxyinosine 47, guanosine 27, 2'-deoxyguanosine 32. The Km-values (μmol l-1) of purine riboside and deoxyriboside synthesis are lower than the values for phosphorolysis (hypoxanthine 18 and 34, resp., guanine 8 and 11, resp.). An affinity lower by one order shows PNP for (-D-ribose-1-phosphate, (-D-2-deoxyribose-1-phosphate (Km = 200 μmol l-1 in both cases) and phosphate (Km = 805 μmol l-1). The substrate specificity of the enzyme was also studied: positions N(1), C(2) and C(8) are decisive for the binding of the substrate (purine nucleoside).

Biochemical studies on the production of neuraminidase by environmental isolates of Vibrio cholerae non-O1 from Bulgaria

2011 ◽  
Vol 57 (7) ◽  
pp. 606-610 ◽  
Author(s):  
Rumyana Eneva ◽  
Stephan Engibarov ◽  
Tanya Strateva ◽  
Radoslav Abrashev ◽  
Ignat Abrashev
Keyword(s):  
Vibrio Cholerae ◽  
Pathogenic Bacteria ◽  
Environmental Isolates ◽  
Anaerobic Conditions ◽  
Temperature Optimum ◽  
Ph Optimum ◽  
Cholera Vibrio ◽  
Key Factor ◽  
Aeration Conditions ◽  
The One

Neuraminidase is a key factor in the infectious process of many viruses and pathogenic bacteria. The neuraminidase enzyme secreted by the etiological agent of cholera — Vibrio cholerae О1 — is well studied in contrast with the one produced by non-O1/non-O139 V. cholerae. Environmental non-O1/non-O139 V. cholerae isolates from Bulgaria were screened for production of neuraminidase. The presence of the neuraminidase gene nanH was detected in 18.5% of the strains. Тhe strain showing highest activity (30 U/mL), V. cholerae non-O1/13, was used to investigate the enzyme production in several media and at different aeration conditions. The highest production of extracellular neuraminidase was observed under microaerophilic conditions, which is possibly related to its role in the infection of intestine epithelium, where the oxygen content is low. On the other hand, this is another advantage of the microbe in such microaerophilic environments as sediments and lake mud. The highest production of intracellular neuraminidase was observed at anaerobic conditions. The ratio of extracellular to intracellular neuraminidase production in V. cholerae was investigated. The temperature optimum of the enzyme was determined to be 50 °C and the pH optimum to be 5.6–5.8.

scholarly journals The Effect of Magnesium Ion Concentration on the pH Optimum of the Spinach Leaf Alkaline Fructose Diphosphatase

1967 ◽  
Vol 242 (9) ◽  
pp. 2292-2294 ◽  
Author(s):  
Jack Preiss ◽  
Martie Louise Biggs ◽  
Elaine Greenberg
Keyword(s):  
Ion Concentration ◽  
Magnesium Ion ◽  
Ph Optimum ◽  
Spinach Leaf
Sign in / Sign up

Export Citation Format

Share Document