scholarly journals A CELLULOLYTIC ENZYME PREPARATION FROM MYROTHECIUM VERRUCARIA

1948 ◽  
Vol 174 (2) ◽  
pp. 697-703
Author(s):  
P.R. Saunders ◽  
R.G.H. Siu ◽  
R.N. Genest
Keyword(s):  
Enzyme Preparation ◽  
Cellulolytic Enzyme ◽  
Myrothecium Verrucaria

scholarly journals Paenibacillus curdlanolyticus Strain B-6 Xylanolytic-Cellulolytic Enzyme System That Degrades Insoluble Polysaccharides

2006 ◽  
Vol 72 (4) ◽  
pp. 2483-2490 ◽  
Author(s):  
Patthra Pason ◽  
Khin Lay Kyu ◽  
Khanok Ratanakhanokchai
Keyword(s):  
Growth Phase ◽  
Enzyme Preparation ◽  
Enzyme System ◽  
Crude Enzyme ◽  
Cellulolytic Enzyme ◽  
Crude Enzyme Preparation ◽  
Multienzyme Complexes ◽  
Sds Page ◽  
Paenibacillus Curdlanolyticus ◽  
Cellulose Binding

ABSTRACT A facultatively anaerobic bacterium, Paenibacillus curdlanolyticus B-6, isolated from an anaerobic digester produces an extracellular xylanolytic-cellulolytic enzyme system containing xylanase, β-xylosidase, arabinofuranosidase, acetyl esterase, mannanase, carboxymethyl cellulase (CMCase), avicelase, cellobiohydrolase, β-glucosidase, amylase, and chitinase when grown on xylan under aerobic conditions. During growth on xylan, the bacterial cells were found to adhere to xylan from the early exponential growth phase to the late stationary growth phase. Scanning electron microscopic analysis revealed the adhesion of cells to xylan. The crude enzyme preparation was found to be capable of binding to insoluble xylan and Avicel. The xylanolytic-cellulolytic enzyme system efficiently hydrolyzed insoluble xylan, Avicel, and corn hulls to soluble sugars that were exclusively xylose and glucose. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of a crude enzyme preparation exhibited at least 17 proteins, and zymograms revealed multiple xylanases and cellulases containing 12 xylanases and 9 CMCases. The cellulose-binding proteins, which are mainly in a multienzyme complex, were isolated from the crude enzyme preparation by affinity purification on cellulose. This showed nine proteins by SDS-PAGE and eight xylanases and six CMCases on zymograms. Sephacryl S-300 gel filtration showed that the cellulose-binding proteins consisted of two multienzyme complexes with molecular masses of 1,450 and 400 kDa. The results indicated that the xylanolytic-cellulolytic enzyme system of this bacterium exists as multienzyme complexes.

scholarly journals Analysis of the chemical composition and properties of the main and side products during the implementation of new technologies for producing ethanol

2020 ◽  
Vol 82 (3) ◽  
pp. 71-77
Author(s):  
N. V. Zueva ◽  
G. V. Agafonov ◽  
I. Y. Lukinova ◽  
A. N. Dolgov
Keyword(s):  
Protein Content ◽  
Crude Protein ◽  
Enzyme Preparation ◽  
Aqueous Suspension ◽  
Feed Additives ◽  
Fiber Content ◽  
Water Soluble ◽  
Cellulolytic Enzyme ◽  
Protein Supplement ◽  
Crude Protein Content

The article studied yeast composition isolated from the separation of the mash, bran separated in the grinding step, as well as a protein supplement obtained by mixing these two products. Crude fat content ranges from 4,7 to 6,2%, crude protein content is 38%, which is 20% lower than in the fodder yeast, but 14% higher than that of the bran. It is also found that the resulting protein product enriched in micro- and macro-elements, as well as readily hydrolyzable and water soluble carbohydrates. crude fiber content is 5,5%, which is almost 2,5 times lower than in the bran. The composition of the feed protein supplement obtained with the introduction at the stage of aqueous suspension of wheat powdery cellulolytic enzyme preparation Viskolaza 150 L and without it. The enzyme preparation was added in the step of preparing aqueous suspensions and wheat powdery dosage of 0,01% by weight of the feedstock. protein feed additives obtained with and without addition of cellulolytic enzyme preparation of high quality crude protein content and protein. Thus, the content of crude protein in the protein with the introduction of an additive in an aqueous suspension of powdery Viskolazy 150 L was 37% whereas 34% without the enzyme preparation. The amount of soluble polysaccharides and the mass fraction of ash were practically at the same level of from 2,4 to 5% and from 5,5 to 7,0%, respectively. fiber content of the protein supplement using Viskolazy 150 L was 4,2-6,1%, which is 2,5 times lower than in the protein supplement obtained without enzyme preparation.

scholarly journals Evaluation of efficiency of using the enzyme preparation «Celloviridin Dx20» in the content of pig feed

2016 ◽  
Vol 7 (1) ◽  
pp. 13-17
Author(s):  
A. O. Dejnega ◽  
V. O. Lesova ◽  
A. S. Anatsky
Keyword(s):  
Plant Cell ◽  
Enzyme Preparation ◽  
The Body ◽  
Farm Animals ◽  
Cellulolytic Enzyme ◽  
Positive Trend ◽  
Feed Mixture ◽  
Enzyme Preparations ◽  
Young Pigs ◽  
Intracellular Proteins

One of the main problems in the feeding of farm animals is the low degree of digestion and assimilation of nutrients in the feed used in animal production. In the bodies of animals such as pigs and poultry enzymes and microflora which are necessary for breaking down cellulose and other polysaccharides of vegetable raw materials are absent, therefore they not only fail to be digested in the gastrointestinal tract, but also obstruct access of other digestive enzymes to the other feed components, in particular intracellular proteins. The only way to solve this problem is deliberate introduction of enzymes into food. Depending on the type and composition of the feed, amylolytic, proteolytic, cellulolytic enzyme preparations are used. The purpose of this work is to assess the effect of the enzyme preparation "Celloviridin Dx20" as a fodder component on the growth and biochemical parameters of young pigs. For this purpose, a scientific and economic experiment on feeding young pigs was conducted at the agro-industrial farm«Niva» (Novonikolaevka village, Dnipropetrovsk region), in which the enzyme preparation «Celloviridin Dx20», which promotes the breakdown of plant cell polysaccharides (cellulose, xylans) was introduced to a standard feed mixture used in swine husbandry. The composition of the ration consisted of 60% barley, 20% wheat and 20% of the protein-vitamin-mineral complex «ShenPigStart». The results of the experiment showed that the introduction into the feed mixture of the enzyme preparation at 100 g per ton helps to increase the body weight of pigs by 11.6% compared to the control, can increase the digestion rate of fibre (13.8%), protein and fat. These results can be explained by the mechanism of action of the enzyme complex, which consists in the hydrolysis of polysaccharides of plant cell walls in the feed in the digestive tract of pigs, the formation of digestable polysaccharides and the release of additional quantities of intracellular proteins. The result of these phenomena is also a positive trend in feed nitrogen assimilation in animals of the experimental group: a 19% decrease in the amount of physiological secretions and a 12.5% increase in nitrogen use. At the same time hematology (hemoglobin, erythrocytes, leukocytes), calcium and phosphorus metabolism remained unchanged. This shows that the preparation used does not accumulate in the body and gradually loses enzymatic activity, and under the influence of the pigs’ stomach proteases it is broken down into separate amino acids which are absorbed by the animals. The resulting stimulatory effect of using "Celloviridin Dх20" has not only physiological but also economic importance, as it helps reduce the time for the pigs to reach slaughter weight (close to 100 kg) by 11 days, and consequently, reduces feed intake and its costs in rearing pigs on farms. Therefore, it is advisable to use "Celloviridin Dх20" in swine husbandry.

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

THE INFLUENCE OF ETHANOL ON THE CONVERSION OF PREGNENOLONE TO PROGESTERONE BY HUMAN PLACENTAL MICROSOMES

1974 ◽  
Vol 76 (1) ◽  
pp. 178-188 ◽  
Author(s):  
H. Lübbert ◽  
K. Pollow ◽  
R. Wagner ◽  
J. Hammerstein
Keyword(s):  
Kinetic Parameters ◽  
Enzyme Preparation ◽  
Ethanol Concentration ◽  
Hydroxysteroid Dehydrogenase ◽  
Product Formation ◽  
Linear Increase ◽  
Maximal Velocity ◽  
Microsomal Enzyme ◽  
Temperature Optima ◽  
Substrate Concentrations

ABSTRACT The effects of ethanol on kinetic parameters of placental Δ5-3β-hydroxysteroid dehydrogenase were studied. In the presence of high pregnenolone concentrations (50 μm, [S] > Km) the microsomal enzyme preparation exhibited an almost linear increase in activity as the ethanol concentration in the medium was raised from 2.5 to 15 % (v/v). At lower substrate concentrations ([S] << Km) ethanol caused inhibition. Other effects of ethanol were: linearity of product formation with time was prolonged; the maximal velocity was markedly increased; the Km for pregnenolone slightly decreased with increasing ethanol concentrations (2.5 to 10 %, v/v) whereas the Km for NAD remained the same. The pH and temperature optima of the reaction were unaffected by ethanol. Other organic solvents caused similar effects.

UDP-D-glucose 4-epimerase activity of the tissue culture of white poplars (Populus alba L. var. pyramidalis)

1982 ◽  
Vol 47 (5) ◽  
pp. 1530-1536 ◽  
Author(s):  
Ladislav Bilisics ◽  
Štefan Karácsonyi ◽  
Marta Kubačková
Keyword(s):  
Tissue Culture ◽  
Cell Walls ◽  
Enzyme Preparation ◽  
Uridine Diphosphate ◽  
Populus Alba ◽  
Activity Change ◽  
White Poplar ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Galactose Content

The presence of UDP-D-glucose 4-epimerase (EC 5.1.3.2) in the culture tissue of white poplar was evidenced. As found, the partially purified enzyme preparation contained UDP-D-glucose glucosyltransferase, UDP-D-galactose galactosyltransferase and non-specific enzymes able to cleave the uridine-diphosphate saccharides into the appropriate hexose monophosphates. The activity change of UDP-D-glucose 4-epimerase in tissue culture cells during the growth was in accord with changes in D-galactose content in cell walls and indicated the possibility to regulate the formation of polysaccharides containing D-galactose at the level of production of UDP-D-galactose in cells.

Mechanism of inhibition of succinate oxidase by products of oxidation of o-dihydroxycoumarins

1980 ◽  
Vol 45 (2) ◽  
pp. 641-652
Author(s):  
Petr Zbořil
Keyword(s):  
Inhibitory Activity ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Inhibitory Effects ◽  
Anaerobic Conditions ◽  
Long Period ◽  
Mechanism Of Inhibition ◽  
Intermediary Product ◽  
Succinate Oxidase ◽  
By Products

Semiquinone is an intermediary product of the oxidation of daphnetin (7,8-dihydroxycoumarin) and esculetin (6,7-dihydroxycoumarin) by diphenol oxidase; its concentration rapidly decreases. When the oxidation is effected by ferricytochrome c, the concentration of the semiquinone remains practically constant for a long period. Similarly, the ability of the products of daphnetin oxidation by diphenol oxidase to inhibit succinate oxidase activity in mitochondrial fragments rapidly decreases with time; the decrease is considerably slower in the case of cytochrome c. The inhibitory activity of the product decreases with time also during esculetin oxidation by ferricyanide. This indicates that the inhibitory effects must be ascribed predominantly to the semiquinone, the quinone is less efficient. The inhibition of succinate oxidase or succinate dehydrogenase was strongly decreased when the enzyme preparation of Keilin and Hartree was incubated with esculetin and ferricyanide in the presence of KCN or under anaerobic conditions. This demonstrates that the reaction of the inhibitor with the enzyme either involves subsequent oxidations or that the inhibitor preferentially reacts with the oxidized form of the sensitive component of the respiratory chain. The second alternative is very little probable since there is no correlation between the degree of inhibition and the binding of the inhibitor to mitochondrial fragments.

scholarly journals Glucuronides Hydrolysis by Intestinal Microbial β-Glucuronidases (GUS) Is Affected by Sampling, Enzyme Preparation, Buffer pH, and Species

Pharmaceutics ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1043
Author(s):  
Christabel Ebuzoeme ◽  
Imoh Etim ◽  
Autumn Ikimi ◽  
Jamie Song ◽  
Ting Du ◽  
...  
Keyword(s):  
Enzyme Preparation ◽  
Reaction System ◽  
Reaction Rates ◽  
Experimental Conditions ◽  
Model Animal ◽  
Fresh Feces ◽  
Time Buffer ◽  
Exogenous Compounds ◽  
Activity Loss ◽  
The Impact

Glucuronides hydrolysis by intestinal microbial β-Glucuronidases (GUS) is an important procedure for many endogenous and exogenous compounds. The purpose of this study is to determine the impact of experimental conditions on glucuronide hydrolysis by intestinal microbial GUS. Standard probe 4-Nitrophenyl β-D-glucopyranoside (pNPG) and a natural glucuronide wogonoside were used as the model compounds. Feces collection time, buffer conditions, interindividual, and species variations were evaluated by incubating the substrates with enzymes. The relative reaction activity of pNPG, reaction rates, and reaction kinetics for wogonoside were calculated. Fresh feces showed the highest hydrolysis activities. Sonication increased total protein yield during enzyme preparation. The pH of the reaction system increased the activity in 0.69–1.32-fold, 2.9–12.9-fold, and 0.28–1.56-fold for mouse, rat, and human at three different concentrations of wogonoside, respectively. The Vmax for wogonoside hydrolysis was 2.37 ± 0.06, 4.48 ± 0.11, and 5.17 ± 0.16 μmol/min/mg and Km was 6.51 ± 0.71, 3.04 ± 0.34, and 0.34 ± 0.047 μM for mouse, rat, and human, respectively. The inter-individual difference was significant (4–6-fold) using inbred rats as the model animal. Fresh feces should be used to avoid activity loss and sonication should be utilized in enzyme preparation to increase hydrolysis activity. The buffer pH should be appropriate according to the species. Inter-individual and species variations were significant.

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