scholarly journals Effects of music playing on biological molecules

2018 ◽  
Vol 210 ◽  
pp. 05006 ◽  
Author(s):  
Catia Algieri ◽  
Claudio Guarnaccia ◽  
Vincenzo Barone ◽  
Maria Raffaella Gullo ◽  
Laura Donato
Keyword(s):  
Enzyme Activity ◽  
Detrimental Effect ◽  
Specific Activity ◽  
Time Lag ◽  
Enzymatic Reaction ◽  
Biological Molecules ◽  
National Council ◽  
Musical Piece ◽  
Tyrosinase Enzyme ◽  
Positive Effect

In this work the effect of two different musical pieces (called “Reminiscenza” and “Pioggia”) on the tyrosinase enzyme activity was investigated. The l-DOPA production by the enzymatic reaction was measured during the continuous playing of these musical pieces. Experiments were performed in the laboratories of the Institute of Membrane Technology (ITM) of the Italian National Council for Research (CNR). The results showed that a positive effect was exercised by the “Reminiscenza” piece, which determined an increase of the specific activity about of 30 % with respect to the value measured in the absence of sound. On the contrary, “Pioggia” piece had a detrimental effect on the enzymatic process. In particular, a time lag on the l-DOPA production, during the first minutes of the reaction, was detected. After this period, an increase of the reaction velocity occurred even if the enzyme activity was lower than the value obtained in the absence of music. These results show that the peculiar characteristics of a musical piece can exercise a positive or negative action on biological elements and open the way to further studies in this area.

scholarly journals Cloning and Expression of Levansucrase Gene of Bacillus velezensis BM-2 and Enzymatic Synthesis of Levan

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 317
Author(s):  
Min Xu ◽  
Lixia Zhang ◽  
Fangkun Zhao ◽  
Jingyue Wang ◽  
Bo Zhao ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Specific Activity ◽  
Enzymatic Reaction ◽  
Production Capacity ◽  
Cloning And Expression ◽  
Buffer System ◽  
Bacterial Strains ◽  
Bacillus Velezensis ◽  
Fusion Enzymes ◽  
Optimal Reaction Temperature

Levan is a versatile and valuable fructose homopolymer, and a few bacterial strains have been found to produce levan. Although levan products have numerous specific functions, their application and promotion were limited by the production capacity and production cost. Bacillus velezensis BM-2 is a levan-synthesizing strain, but its levan production is too low to apply. In this study, the levansucrase gene of B. velezensis BM-2 was cloned to plasmid pET-32a-Acma-zz, and the recombinant plasmids were transferred to Escherichia coli BL21. A transformed clone was selected to express and secrete the fusion enzymes with an Acma-tag efficiently. The expressed products were further purified by a self-developed separating material called bacterial enhancer matrix (BEM) particles. The purification efficiency was 93.4%, with a specific activity of 16.589 U/mL protein. The enzymatic reaction results indicated that the optimal reaction temperature is 50 °C, the optimal pH of the acetate buffer is 5.6, and the buffer system greatly influenced the enzyme activity. The enzyme activity was enhanced to 130% in the presence of 5 mM Ca2+, K+, Zn2+, and Mn2+, whereas it was almost abolished in the case of Cu2+ and Fe3+. The values of Km, kcat, and kcat/Km were 17.41 mM, 376.83 s−1, and 21.64 mM−1s−1, respectively. The enzyme amount of 20 U/g sucrose was added to the system containing 400 g/L sucrose, and the levan products with a concentration of 120 g/L reached after an incubation of 18 h, which was 8 times that of the yield before optimization. The results of molecular docking analysis indicated that the Asp86 might act as a nucleophilic catalytic residue for sucrose, Arg246 and Asp247 act as transition state stabilizer of transfructosylation, and Glu340 and Arg306 were recognized as general acid donors. They formed the catalytic-groups triad. The unique properties and catalytic activity of the levansucrase suggest that it deserves further research and might have good industrial application prospects.

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 Study of Extraction and Enzymatic Properties of Cell-Envelope Proteinases from a Novel Wild Lactobacillus plantarum LP69

Catalysts ◽  
2018 ◽  
Vol 8 (8) ◽  
pp. 325 ◽  
Author(s):  
He Chen ◽  
Jie Huang ◽  
Binyun Cao ◽  
Li Chen ◽  
Na Song ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Lactobacillus Plantarum ◽  
Industrial Development ◽  
Extraction Efficiency ◽  
Specific Activity ◽  
Cell Envelope ◽  
Serine Proteinase ◽  
Kinetic Studies ◽  
Predicted Values ◽  
Hydrolyze Whey Protein

Lactobacilli cell-envelope proteinases (CEPs) have been widely used in the development of new streams of blockbuster nutraceuticals because of numerous biopharmaceutical potentials; thus, the development of viable methods for CEP extraction and the improvement of extraction efficiency will promote their full-scale application. In this study, CEP from a novel wild Lactobacillus plantarum LP69 was released from cells by incubating in calcium-free buffer. The extraction conditions of CEP were optimized by response surface methodology with the enzyme activity and specific activity as the detective marker. The optimal extraction conditions were: time of 80 min, temperature of 39 °C and buffer pH of 6.5. Under these conditions, enzyme activity and specific activity were (23.94 ± 0.86) U/mL and (1.37 ± 0.03) U/mg, respectively, which were well matched with the predicted values (22.12 U/mL and 1.36 U/mg). Optimal activity of the crude CEP occurred at pH 8.0 and 40 °C. It is a metallopeptidase, activated by Ca2+, inhibited by Zn2+ and ethylene-diamine-tetra-acetic acid, and a serine proteinase which is inhibited by phenylmethylsulfonyl fluoride. Kinetic studies showed that CEP from LP69 could hydrolyze whey protein, lactoglobulin and casein. Our study improves the extraction efficiency of CEPs from LP69, providing the reference for their industrial development.

Enzymatic condensation of dopamine and acetaldehyde: a salsolinol synthase from rat brain

Biologia ◽  
2011 ◽  
Vol 66 (6) ◽  
Author(s):  
Xuechai Chen ◽  
Abida Arshad ◽  
Hong Qing ◽  
Rui Wang ◽  
Jianqing Lu ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Substantia Nigra ◽  
Human Subjects ◽  
Enzymatic Reaction ◽  
Brain Regions ◽  
Activity Detection ◽  
Reaction Products ◽  
Sprague Dawley ◽  
Sprague Dawley Rats ◽  
Salsolinol Synthase

AbstractSalsolinol (1-methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline; Sal) is structurally similar to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, which is supposed to have a role in the development of Parkinson-like syndrome in both human and non-human subjects. In the human brain, the amount of (R)-enantiomer of Sal is much higher than (S)-enantiomer, suggesting that a putative enzyme may participate in the synthesis of (R)-salsolinol, called (R)-salsolinol synthase. In this study, the (R)-salsolinol synthase activity in the condensation of dopamine and acetaldehyde was investigated in the crude extracts from the brains of Sprague Dawley rats. Identification of the enzymatic reaction products and enzyme activity detection were achieved by HPLC-electrochemical detection. The discovery of this enzyme activity in rat’s brain indicates the natural existence of (R)-salsolinol synthase in the brains of humans and rats, and it is distributed in most brain regions of rat with higher activity in soluble proteins extracted from striatum and substantia nigra.

Binding of 3-phosphoglycerate leads to both activation and stabilisation of ADP-glucose pyrophosphorylase from apple leaves

2005 ◽  
Vol 32 (9) ◽  
pp. 839
Author(s):  
Rui Zhou ◽  
Lailiang Cheng
Keyword(s):  
Heat Treatment ◽  
Thermal Stability ◽  
Enzyme Activity ◽  
Inorganic Phosphate ◽  
Thermal Inactivation ◽  
Specific Activity ◽  
Apple Leaves ◽  
Apparent Homogeneity ◽  
Adp Glucose Pyrophosphorylase ◽  
High Concentrations

Apple leaf ADP-glucose pyrophosphorylase was purified 1436-fold to apparent homogeneity with a specific activity of 58.9 units mg–1. The enzyme was activated by 3-phosphoglycerate (PGA) and inhibited by inorganic phosphate (Pi) in the ADPG synthesis direction. In the pyrophosphorolytic direction, however, high concentrations of PGA (> 2.5 mm) inhibited the enzyme activity. The enzyme was resistant to thermal inactivation with a T0.5 (temperature at which 50% of the enzyme activity is lost after 5 min incubation) of 52°C. Incubation with 2 mm PGA or 2 mm Pi increased T0.5 to 68°C. Incubation with 2 mm dithiothreitol (DTT) decreased T0.5 to 42°C, whereas inclusion of 2 mm PGA in the DTT incubation maintained T0.5 at 52°C. DTT-induced decrease in thermal stability was accompanied by monomerisation of the small subunits. Presence of PGA in the DTT incubation did not alter the monomerisation of the small subunits of the enzyme induced by DTT. These findings indicate that binding of PGA renders apple leaf AGPase with a conformation that is not only more efficient in catalysis but also more stable to heat treatment. The physiological significance of the protective effect of PGA on thermal inactivation of AGPase is discussed.

scholarly journals Induction of carnitine acetyltransferase by clofibrate in rat liver

1981 ◽  
Vol 194 (1) ◽  
pp. 249-255 ◽  
Author(s):  
B Mittal ◽  
C K R Kurup
Keyword(s):  
Protein Synthesis ◽  
Enzyme Activity ◽  
Rat Liver ◽  
Time Lag ◽  
Mitochondrial Protein ◽  
Carnitine Acetyltransferase ◽  
Enzyme Protein ◽  
General Protein Synthesis ◽  
Liver And Kidney ◽  
General Protein

Administration of the anti-hypercholesterolaemic drug clofibrate to the rat increases the activity of carnitine acetyltransferase (acetyl-CoA-carnitine O-acetyltransferase, EC 2.3.1.7) in liver and kidney. The drug-mediated increase in enzyme activity in hepatic mitochondria shows a time lag during which the activity increases in the microsomal and peroxisomal fractions. The enzyme induced in the particulate fractions is identical with one normally present in mitochondria. The increase in enzyme activity is prevented by inhibitors of RNA and general protein synthesis. Mitochondrial protein-synthetic machinery does not appear to be involved in the process. Immunoprecipitation shows increased concentration of the enzyme protein in hepatic mitochondria isolated from drug-treated animals. In these animals, the rate of synthesis of the enzyme is increased 7-fold.

5α-Reductase activity in stroma and epithelium of rat prostate and epididymis. A contribution to elucidation of the mechanism for development of hyperplastic growth of prostatic tissue

1983 ◽  
Vol 103 (2) ◽  
pp. 273-281 ◽  
Author(s):  
Ole Djøseland ◽  
Nicholas Bruchovsky ◽  
Paul S. Rennie ◽  
Navdeep Otal ◽  
Sian Høglo
Keyword(s):  
Enzyme Activity ◽  
Specific Activity ◽  
Reductase Activity ◽  
Major Change ◽  
Growth Stimulation ◽  
Total Activity ◽  
Prostatic Tissue ◽  
Ventral Prostate ◽  
Total Enzyme Activity ◽  
Abnormal Growth

Abstract. The 5α-reductase activity was assayed in homogenates of stroma and epithelium in the rat ventral prostate and epididymis. Samples consisting of 0.3 mg/ml tissue protein in TES buffer, pH 7.0 were incubated at 37°C for 30 min in the presence of 50 nm [1,2-3H]testosterone and a NADPH-generating system started with 5 × 10−4 m NADP. The yield of 5α-reduced metabolites, as established by using thin-layer chromatography, gave an estimate of enzyme activity. Whereas the specific activity of 5α-reductase was highest in prostatic stroma and epididymal epithelium, most of the total enzyme activity was associated with the epithelium in both the prostate and epididymis. The effect of dihydrotestosterone on specific activity of 5α-reductase was studied by administering the hormone to 7-day castrated rats. In prostate, the specific activity of both stromal and epithelium forms of the enzyme reached a maximum after 4 days of treatment. In epididymis only the epithelial form of 5α-reductase underwent a major change in specific activity, the latter peaking after 8–12 days of treatment. Furthermore, while the total activity of 5α-reductase in the prostatic tissue fractions could be induced by as much as 4-fold the normal control values, the epididymal enzyme could not be induced above the normal level either in the stroma or the epithelium. This may explain the relative resistance of epididymis to abnormal growth stimulation under the influence of hormones.

scholarly journals SELECTED PROTEOLYTIC ACTIVITY BY EXTRACTS OF DERMESTID LARVAE

2011 ◽  
Vol 19 (19) ◽  
pp. 79-83
Author(s):  
Lavinel G. IONESCU
Keyword(s):  
Enzyme Activity ◽  
Ammonium Sulfate ◽  
Proteolytic Activity ◽  
Specific Activity ◽  
Proteolytic Enzymes ◽  
High Specific Activity ◽  
Water Extract ◽  
Dermestes Maculatus ◽  
Crude Preparation

The larvae of the Beetle Dermestes maculatus De Geer can subsist on a diet consisting largely of protein. Studies have been undertaken to investigate the nature of proteolytic enzymes. A water extract of the larvae yielded a crude preparation that hydrolyzes gelatin, bide powder, hemoglobin substrate, benzoyl-DL-arginine p-nitroamilide, and glutaryl-L-phenylalanine p-nitroanilide. Enzyme activity was found in a non-dialyzable, heat- and acid0labile portion of the extract yielded two fractions with high specific activity towards gelatin. These are precipitated between 40% to 60% saturation of ammonium sulfate and 60% to 80% saturation. The higher specific activity was observed in the 40%-60% fraction. These results suggest that the larvae of these dermestids contain proteolytic enzymes with actions similar to mammalian trypsin and chymotrypsin. The results also suggest that other proteolytic enzymes may be present as well.

scholarly journals Comparative assessment of microbial enzyme activity with compost and sewage sludge amendment

2015 ◽  
Vol 7 (2) ◽  
pp. 1021-1028
Author(s):  
Jatinder Kaur ◽  
Sandeep Sharma ◽  
Hargopal Singh
Keyword(s):  
Enzyme Activity ◽  
Sewage Sludge ◽  
Organic Carbon ◽  
Soil Microbial Activity ◽  
Available Phosphorus ◽  
Microbial Activities ◽  
Soil Microbial ◽  
Microbial Enzyme ◽  
Positive Effect ◽  
Digested Sewage Sludge

Changes in soil microbial activities were investigated to examine the effect of aerobically digested sewage sludge (SS) and compared with compost under incubation conditions over 63 days. Sandy soil was amended with 0.25, 0.5, 1.0 and 1.5 % w/w of compost and sewage sludge. Enzyme activity (dehydrogenase, alkaline phosphatase, acid phosphatase, phytase and urease) were examined at an interval of 3, 7, 14, 21, 28, 42 and 63 days. At the end of the experiment the change in organic carbon, nitrogen, potassium and phosphorus was also recorded.Results indicated that enzyme activities were substantially enhanced in presence of both amendments for first few days and the higher increases were measured at 1.5% of compost and sewage sludge amendment. Then an overall decrease in enzyme activity was recorded. Both the amendments also significantly increased the organic carbon, nitrogen and potassium of the soil while increase in available phosphorus was only recorded in treatment receiving compost. The present experiment indicated that addition of compost and sewage sludge have positive effect on soil microbial activity and can be safely used as soil amendment without having any adverse effect. Though, a previous examination of sewage sludge to be used must be made for heavy metals and pathogens.

scholarly journals Pre-fermentative treatment of a model wine with aim to serve as a functional food with decreased alcohol content

2017 ◽  
Vol 63 (01) ◽  
pp. 47-53
Author(s):  
Irina Mladenoska ◽  
Verica Petkova ◽  
Tatjana Kadifkova Panovska
Keyword(s):  
Enzyme Activity ◽  
Gluconic Acid ◽  
Functional Food ◽  
Ph Value ◽  
Enzymatic Reaction ◽  
Alginate Beads ◽  
High Concentration ◽  
Ph Optimum ◽  
Enzyme Preparations ◽  
Initial Ph

The effect of substrate concentration on the enzyme activity in the reaction of glucose conversion into gluconic acid was investigated by using three different enzyme preparations in media with two different glucose concentrations. The media were simulating the conditions in the must, thus named as minimal model must, and were composed form combination of several organic acids and glucose. Those media were having initial pH of 3.5 that is a very unfavorable for glucose oxidase activity having a pH optimum at the pH value of 5.5. Among the three preparations used, the bakery additive, Alphamalt Gloxy 5080, was the most active in the medium with glucose concentration of 10 g/L, showing conversion of more than 70% for the period of 24 h, while the same enzyme preparation in the medium with 100 g/L glucose converted only about 7% of glucose. The pH value of the medium at the beginning and at the end of the enzymatic reaction was a good indicator of the enzyme activity. It seems that for the conversion of glucose in higher concentration, enzymatic preparation in high concentration should also be used. The preliminary attempt of immobilization of two preparations of glucose oxidases in alginate beads was also performed and a successful immobilization procedure for utilization in food industry was preliminarily developed. Keywords: glucose oxidases, enzymatic pretreatment, glucose, gluconic acid, model wine, functional food

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