MEMBRAN POLYETHERSULFONE DAN REGENERATED CELLULOSE UNTUK ULTRAFILTRASI

2012 ◽  
Vol 11 (2) ◽  
Author(s):  
Trismilah Trismilah ◽  
Achmadin Lutfi
Keyword(s):  
Enzyme Activity ◽  
Protein Content ◽  
Bacillus Stearothermophilus ◽  
Specific Activity ◽  
Ultrafiltration Membrane ◽  
Regenerated Cellulose ◽  
Cellulose Membrane ◽  
Membrane Process ◽  
Purification Method ◽  
Enzyme Specific Activity

Purification of xilanase result of fermentation from Bacillus stearothermophilus DSM 22 using membrane polyethersulfone and regenerated cellulose, each measuring 30 kD. Variations in pH 4.94, 5.80, 6.60, 7.40, 8.20. Analysis of enzyme activity, protein content and enzyme specific activity carried out on permeate and retentate. This study aimed to learn the best pH condition and the appropriate type of membrane process in the purification method xilanase with ultrafiltrasi. Research of resultsindicate that pH is very influential in the process ultrafiltration xilanase, each membrane has a different characteristic. Purification xilanase best use of ultrafiltration membrane polyethersulfone achieved in the pH 4.94 with a specific activity 13,888 U / mg in the permeate. Purification xilanase best ultrafiltration use of regenerated cellulose membrane at pH 8.20 achieved with specific activity 12397 U / mg in the retentate.

scholarly journals PEMANFAATAN PERLIT YANG TELAH DIMODIFIKASI UNTUK AMOBILISASI ENZIM BROMELAIN

2015 ◽  
Vol 3 (1) ◽  
pp. 40
Author(s):  
Elida Mardiah
Keyword(s):  
Enzyme Activity ◽  
Protein Content ◽  
Incubation Time ◽  
Specific Activity ◽  
Native Enzyme ◽  
Enzymes Activity ◽  
Lowry Method ◽  
Enzyme Specific Activity

 ABSTRACT Amobilization of bromelaine enzyme extracted from ananas fruit (Ananas comusus) acetone has been done. Modified perlite in the amino silica phosphat (ASP) is used as matrix amobilization.  The protein content has determined by Lowry method, while enzyme activity were determined by Anson method caseine as substrate. It native enzyme specific activity was 0.1281 unit/mg with konsentration 20000 ppm, pH 7.0, incubation time 35 minutes, and  temperature 40°C. Amobil bromelaine specific activity was 0.7438 units/mg with substrate on 20000 ppm pH 7.0, incubation time 30 minutes and temperature 37°C. This bromelaine enzymes activity was increased six times than native enzim and showed the activity for several repeatation. Keywords: perlit, enzim bromelain, amobilization

scholarly journals Produksi Enzim Selulase Kasar dari Isolat Bakteri B2S8 menggunakan Substrat Brangkasan Jagung dengan Perlakuan Konsentrasi Inokulum dan Komposisi Media yang berbeda

2020 ◽  
Vol 8 (2) ◽  
pp. 267
Author(s):  
Nursatria Purba ◽  
Ida Bagus Wayan Gunam ◽  
I Made Mahaputra Wijaya
Keyword(s):  
Enzyme Activity ◽  
Protein Content ◽  
Corn Stover ◽  
Bacterial Isolate ◽  
Specific Activity ◽  
Block Design ◽  
Cellulolytic Bacteria ◽  
Endoglucanase Activity ◽  
Cellulase Enzyme ◽  
The Media

The purpose of this study was determined the media and concentration of cellulolytic bacterial isolates to produce high cellulase enzyme activity. Production of crude cellulase enzyme in media and concentration of different bacterial isolate used a factorial Randomized Block Design (RBD) which consist of two factors. The first factor was the media production of different cellulase enzyme consisting of 3 levels, namely media 1, 2 and 3. The second factor was the concentration of bacterial isolate consisting of 5 levels namely 1, 2, 3, 4 and 5%. This study used a B2S8 cellulolytic bacterial isolate that has the highest value of cellulase enzyme activity and the highest degradation rate of cellulose in previous studied and determined the ability of exoglucanase enzyme activity, endoglucanase enzyme and dissolved protein content produced from cellulolytic bacterial isolate. This study used Carboxymethyl Cellulose (CMC) for enzyme activity test and 1% corn stover as a substrate on the media to produce crude cellulase enzyme. The result showed that the highest cellulase enzyme activity in the third media and 5% cellulolytic bacterial inoculum concentration resulted in endoglucanase activity of 0.0332 IU/mL, exoglucanases enzyme activity of 0.0060 IU/mL, dissolved protein content in the amount of 0.5670 mg/mL, the specific endoglucanase activity of 0.0807 IU/mg and the specific activity of exoglucanase of 0.0123 IU/mg. Keywords: Cellulolytic bacteria, Cellulase enzymes, Enzyme activity, Corn stover

Distribution of the multiple molecular forms of glucose-6-phosphate dehydrogenase in different physiological states

1979 ◽  
Vol 57 (5) ◽  
pp. 396-401 ◽  
Author(s):  
Hsiao-Lin Chang ◽  
Darold Holten ◽  
Rom Karin
Keyword(s):  
Enzyme Activity ◽  
Mammary Gland ◽  
Rat Liver ◽  
Specific Activity ◽  
Molecular Forms ◽  
Polyacrylamide Gels ◽  
Multiple Molecular Forms ◽  
Pregnancy And Lactation ◽  
Enzyme Specific Activity ◽  
Glucose 6 Phosphate Dehydrogenase

The distribution of the multiple molecular forms of rat liver and mammary gland glucose-6-phosphate dehydrogenase was determined by electrophoresis on 5% polyacrylamide gels. In both of these organs, changes in the distribution of enzyme activity among the several forms was slight even when approximately 20- to 40-fold changes in enzyme specific activity were achieved by fasting-refeeding experiments (for liver) or during pregnancy and lactation (for mammary gland), it was concluded that the induction of glucose-6-phosphate dehydrogenase in these two organs occurs without any major redistribution among the multiple molecular forms of this enzyme.

Rat prostatic acid phosphatase: androgenic control of isoelectric focusing patterns

1983 ◽  
Vol 61 (7) ◽  
pp. 744-749 ◽  
Author(s):  
J. Downey ◽  
D. Mahan ◽  
T. G. Flynn ◽  
C. E. Bird ◽  
A. F. Clark
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Isoelectric Focusing ◽  
Specific Activity ◽  
Electrophoretic Pattern ◽  
Prostatic Acid Phosphatase ◽  
Staining Intensity ◽  
Adult Rats ◽  
Enzyme Specific Activity ◽  
Ph Range

To further characterize the androgen dependence of prostatic acid phosphatase (AP), the isoelectric focusing patterns of enzyme activity have been examined for normal and castrated adult rats and for rats receiving androgen injections. Isoelectric focusing was performed in polyacrylamide gels over the pH range 4–8. Naphthyl phosphate was used as substrate for staining. For normal rats there was a single lysosomal band (isoelectric point (pI) = 7.35 ± 0.04), four closely migrating secretory bands (pI = 5.96–5.63), and an androgen-dependent band (pI = 6.37 ± 0.05) which as yet has not been identified as either lysosomal or secretory. Following castration the secretory bands decreased significantly in staining intensity, the androgen-dependent band disappeared, and two new lysosomal bands (pI's = 7.13 ± 0.03 and 7.00 ± 0.03) appeared. With androgen replacement the latter two bands disappeared, the androgen-dependent band reappeared, and the secretory bands increased in staining intensity but with the most anodic of the four appearing before the others. This suggests that it could be a precursor to the others. The isoelectric focusing patterns of AP activity appear to be a better method of assessing the androgen status of the prostate than are the previously used parameters, namely, enzyme specific activity, degree of inhibition by tartrate, and polyacrylamide gel electrophoretic pattern.

Immobilization of Peroxidase from Cauliflower Stem on Ultrafiltration Membrane for Phenol Removal

2018 ◽  
Vol 879 ◽  
pp. 137-143
Author(s):  
Karnika Ratanapongleka ◽  
Apinya Onsarn
Keyword(s):  
Membrane Filtration ◽  
Enzymatic Reaction ◽  
Covalent Bonding ◽  
Ultrafiltration Membrane ◽  
Regenerated Cellulose ◽  
Cellulose Membrane ◽  
Phenol Removal ◽  
Permeate Flux ◽  
Reaction Efficiency ◽  
Enzyme Leakage

The aim of this work is to investigate phenol removal by immobilized peroxidase extracted from cauliflower stem. Peroxidase was partially purified by membrane filtration and diafiltration. Almost four-fold increase in the measured activity of partially purified peroxidase was obtained. The enzyme was then immobilized on to the surface of regenerated cellulose ultrafiltration membrane (molecular weight cut-off 30 kDa) using a dead-end filtration unit. Three different immobilization methods (physical adsorption, cross-linking and covalent-bonding using glutaraldehyde as a membrane activator) were tested. The immobilization and enzymatic reaction efficiency were evaluated in terms of the immobilization yield, the enzyme leakage from the system, the phenol removal and the permeate flux. Results showed that the immobilization methods did not much affect the permeate flux of the membrane. The peroxidase immobilization by covalent-bonding on regenerated cellulose membrane produced the highest immobilization yield and the lowest enzyme leakage. The immobilized enzymatic reaction efficiency on phenol removal was 100% at operational time 60 min and reduced to 96.4% at 600 min.

scholarly journals PRODUKSI DAN PENENTUAN KONDISI OPTIMUM ENZIM XILANASE Bacillus amyloliquefaciens FUKUMOTO PADA SUBSTRAT XILAN JERAMI

2015 ◽  
Vol 2 (1) ◽  
pp. 74
Author(s):  
Widiyanti Sekatresna ◽  
Abdi Dharma ◽  
Periadnadi
Keyword(s):  
Enzyme Activity ◽  
Rice Straw ◽  
Incubation Time ◽  
Substrate Concentration ◽  
Bacillus Amyloliquefaciens ◽  
Specific Activity ◽  
Enzymatic Reaction ◽  
Optimal Conditions ◽  
Enzyme Specific Activity

 ABSTRACT The production and determination of  optimal condition of xylanase produced by Bacillus amyloliquefaciens on rice straw xylan were investigated in this study. The parameters to be observed were optimal conditions of pH, temperature, substrate concentration and incubation time. Xilanase activity was determined by measuring the amount of reducing sugar formed in the enzymatic reaction based on Somogyi Nelson method. Optimal conditions needed for the production of xylanase were at pH 7, temperature 27°C and six days of incubation time. While optimal conditions of xylanase action were reached at pH 8.2, temperature 45°C, substrate concentration 3.5%(w/w) and 15 minutes of incubation time with enzyme activity and enzyme specific activity of 1.285 U/mL and 0.738 U/mg respectively. As a comparison, xylanase was also produced on pure xylan  (birchwood), enzyme activity and enzyme specific activity obtained were 2.701 U/mL and 1.658 U/mg respectively. Cellulase content in enzyme produced on rice straw xilan showed the enzyme activity of 0.094 U/mL.  Keywords : xylanase, Bacillus amyloliquefaciens, rice straw xilan

scholarly journals Studies on Anti-Cancer Activity of Lysyl Oxidase from Trichoderma Viride MTCC 167

2016 ◽  
Vol 4 (1) ◽  
pp. 57-63
Author(s):  
Shipra Kalra ◽  
Kanav Midha ◽  
Monika ◽  
Manpreet Kaur
Keyword(s):  
Enzyme Activity ◽  
Protein Content ◽  
Ammonium Sulphate ◽  
Specific Activity ◽  
Lysyl Oxidase ◽  
Trichoderma Viride ◽  
Effect Of Temperature ◽  
Ovarian Cancer Cells ◽  
Acetone Precipitation ◽  
Ammonium Sulphate Precipitation

Lysyl oxidase produces H2O2 i.e. ROS by acting on L-Lysyine. In the present study, ROS thus produced has been used by in vitro cytotoxicity assay on ovarian cancer cells thereby achieving 250 percent inhibition. Lysyl oxidase activity was determined spectrophotometrically by Dintrophenylhydrazine (DNPH) reagent. For isolation of lysyl oxidase produced by Trichodermaviride, acetone precipitation and ammonium sulphate precipitation was carried out. The effect of temperature on lysyl oxidase production was determined by incubating the media with 1.5 % inoculum at different temperature ranging from  10 , 20, 30,40,50,60,70 , 80 0C for 72 hr . Anti-tumor properties of Lysyl oxidase was checked using Rhodamine assay and NBT Assay.  Comparative results for Acetone and Ammonium Sulphate precipitation showed that Enzyme activity(U/ml)  of acetone precipitation is 124.6 and 144.3 IU/ml and Protein Content is 1.8 and 2.2 mg/ml with the specific activity 68.4IU/mg and 64.1IU/mg . The optimum enzyme production was found to be at pH 8 and optimum temperature for lysyl oxidase production was 500C with maximum enzyme activity of 0.38 (U/ml). 7th fraction contained highest enzyme activity so the retention time of lysyl oxidase was found to be 7 min. The protein content was also calculated by using Bradford method and it was highest in the 1st fraction and in 6th, 7th and 8th fractions. The specific activity has been improved from 75.1 IU/mg to 86.5 IU/mg. 10 units of lysyl oxidase inhibits 3x104 cells in each well to 82.5% and inhibition achieved at same cell count at 200 units which was 250% as observed with NBT and Rhodamine assay.Int J Appl Sci Biotechnol, Vol 4(1): 57-63

scholarly journals The Organ Distribution, Characterization and Modification of Acetylcholinesterase Activity in Adult African Grasshopper: Zonocerus sp Linn.

2019 ◽  
pp. 1-9
Author(s):  
E. A. Fajemisin ◽  
O. S. Bamidele ◽  
S. O. Ogunsola ◽  
E. A. Aiyenuro
Keyword(s):  
Enzyme Activity ◽  
Protein Content ◽  
Active Site ◽  
Ache Activity ◽  
Specific Activity ◽  
Acetylcholinesterase Activity ◽  
Organ Distribution ◽  
Enzyme Active Site ◽  
University Of Technology ◽  
Tryptophan Residues

Aim: To determine the organ distribution and characterization of acetylcholinesterase in the adult African variegated grasshoppers – Zonocerus variegatus and Zonocerus elegans. (Zonocerus Sp. Linn) Place and Duration of the Study: The insect model: African variegated grasshoppers are gotten from the Open green fields at the Federal University of Technology, Akure, Nigeria, and research was carried out between March and June, 2016 in the Enzymology laboratory, Biochemistry department, Federal University of Technology, Akure, Nigeria. Methodology: Twenty (20) adults variegated grasshoppers were taken from the Open field in the University community, and taken to the Biology department for Identification. After identification, the specimen was weighed, freeze, dissected into fractions (Head, Thorax and Abdomen) and then homogenized to get the crude protein extract. The crude enzyme extract is further purified using the Ion-exchange chromatography with column bed packed with DEAE – Sephadex A50. The protein content of the purified AChE was determined using the Lowry method while the Acetylcholinesterase activity was determined by the Ellman’s assay procedures. The characterization of AChE was tested by modifying agent such as N-Bromo Succinamide (NBS) which confirms the presence of key aromatic proteins involve in catalysis at the active site of the enzyme. Results: The protein concentration according to their fractions: Head (35.7%), Thorax (29.2%), and Abdomen (35.1%). The AChE activity according to their fractions: Head (38.6%), Thorax (23.7%), and Abdomen (37.7%). The specific activity which relates the AChE activity to protein content is given: Head (28.8%), Thorax (40.4%), and Abdomen (30.8%). From the Organ distribution and AChE activity, it was observed that the Head Fractions has the Highest protein content, and Enzyme activity. Comparatively, there are slight differences in the Enzyme activity of the Head and Abdominal fractions which represents the two peaks in the AChE chart. As well, the thorax has the highest specific activity. The modification by the chemical agent NBS shows a drastic decrease (about 50%) in Enzyme activity and characterize enzyme active site with aromatic proteins especially tryptophan residues. Conclusion: Research findings shows the dominance of AChE protein in the Head region, hence high enzyme activity (useful for nervous coordination) as well as presence of tryptophan residues at the enzyme active site. The importance of research is useful in enzymology, neuroscience and public health.

QUANTITATIVE STUDIES OF HYDROLYTIC ENZYME ACTIVITY IN THE SALIVARY GLAND OF CHIRONOMUS TENTANS (DIPTERA: CHIRONOMIDAE) DURING METAMORPHOSIS

1971 ◽  
Vol 103 (3) ◽  
pp. 454-457 ◽  
Author(s):  
Hans Laufer ◽  
Ki Ssu Schin
Keyword(s):  
Enzyme Activity ◽  
Salivary Gland ◽  
Acid Phosphatase ◽  
Protein Content ◽  
Lysosomal Enzymes ◽  
Specific Activity ◽  
Hydrolytic Enzyme ◽  
Hydrolytic Enzymes ◽  
Chironomus Tentans ◽  
Quantitative Studies

AbstractChanges in the hydrolytic enzymes, ribonuclease and acid phosphatase were investigated in the salivary gland of Chironomus tentans since these lysosomal enzymes may participate in hormonally stimulated tissue breakdown. Quantitative assays revealed 9- and 12-fold increases in the specific activity of these enzymes during pupation while the protein content of the gland was decreasing. These increases cannot be accounted for by decreased protein but may represent an activation, accumulation, or synthesis which seems to be important in gland breakdown at metamorphosis.

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