scholarly journals Application of β-glucosidase Immobilized on Chitosan microspheres in Degradation of Polydatin in Polygonum cuspidatum

2021 ◽  
Vol 233 ◽  
pp. 02034
Author(s):  
Wei Zong ◽  
Shan Liu ◽  
Jeonyun Yun ◽  
Xiong Xiao ◽  
Zujun Deng ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cost Reduction ◽  
Degradation Rate ◽  
Temperature Stability ◽  
Catalytic Efficiency ◽  
Efficient Production ◽  
Polygonum Cuspidatum ◽  
Optimum Temperature ◽  
Preparation Conditions ◽  
Hydrolysis Of

Resveratrol in Polygonum cuspidatum is a β-glycoside, which can be hydrolyzed to resveratrol by β-glucosidase. it is an efficient production process to degrade polydatin from Polygonum cuspidatum extract by immobilized β-glucosidase. It is of great significance to explore suitable immobilization conditions to improve the catalytic efficiency and reusability of β-glucosidase for polydatin degradation and cost reduction. In this paper, the recombinant Escherichia coli bgl2238, which was screened and constructed from corn soil of Heilongjiang Province in the early laboratory, was immobilized by chitosan adsorption and glutaraldehyde crosslinking. The preparation conditions and immobilization process of bgl2238 were determined by single factor method: the optimal crosslinking time was 1 h, the optimal crosslinking temperature was 20 °C, the recovery rate of enzyme activity of bgl2238 was 87 %, and the enzyme activity was 859.65 mU/g. The optimum temperature of the immobilized bgl2238 is 50 °C, which is 6 °C higher than that of the free bgl2238, and the temperature stability and pH stability are improved. After six consecutive hydrolysis of Polygonum cuspidatum, the degradation rate of polydatin is still over 70 %, which proves that the immobilized bgl2238 has good reusability. This will be helpful to evaluate the application prospect of β - glucosidase immobilized in this system and determine the best conditions for its production.

scholarly journals Characterization and Effects of β–Galactosidase in the Crude Extracts of Cuminum cyminum and Curcuma longa in Preparation of Delactosed Milk and Whey

2016 ◽  
Vol 5 (1) ◽  
pp. 1
Author(s):  
Omar M. Atrooz
Keyword(s):  
Enzyme Activity ◽  
Curcuma Longa ◽  
Maximum Activity ◽  
Cow’S Milk ◽  
Enzyme Kinetic ◽  
Optimum Temperature ◽  
Cuminum Cyminum ◽  
Crude Extracts ◽  
Optimum Ph ◽  
Hydrolysis Of

<p>β-galactosidase (EC 3.2.1.23) was extracted from <em>Cuminum cyminum </em>and<em> Curcuma longa</em>. The crude extracts of these plants were then characterized in term of pH, temperature, and enzyme kinetic. The crude extracts were also used in hydrolysis of lactose in milk and whey. The enzyme activity was measured by its ability to hydrolyze the substrate o-nitrophenyl β -D-galactopyranoside (ONPG).</p><p>It was found that β-galactosidase in the crude extracts of <em>Cuminum cyminum </em>exhibited maximum activity at pH 8.0 and optimum temperature at 60 °C. While, β-galactosidase in the crude extracts of <em>Curcuma longa</em> have optimum pH at 5.0 and 7.0 and optimum temperature at 50 °C.The K<sub>m</sub> and V<sub>max</sub> values of the β-galactosidase in the crude extracts of <em>Cuminum cyminum</em> and <em>Curcuma longa </em>were 4.16 mM and 0.087 μmol/min, and 2.63 mM and 0.333μmol/min, respectively.</p><p>The results showed that 96.84-97.08% of lactose was hydrolyzed in cow’s milk and whey when treated with crude extracts of <em>Cuminum cyminum</em> and 90-98.6% when treated with crude extracts of <em>Curcuma longa</em>.</p>

THE HYDROLYSIS OF MONOPHOSPHOINOSITIDE BY EXTRACTS OF BRAIN

1967 ◽  
Vol 45 (6) ◽  
pp. 853-861 ◽  
Author(s):  
W. Thompson
Keyword(s):  
Fatty Acids ◽  
Enzyme Activity ◽  
Calcium Ions ◽  
Brain Extract ◽  
Monovalent Cations ◽  
High Concentration ◽  
Diffusible Factor ◽  
Hydrolysis Of ◽  
The Brain ◽  
Long Chain

The hydrolysis of monophosphoinositide by soluble extracts from rat brain is described. Diglyceride and inositol monophosphate are liberated along with a small amount of free fatty acids. Hydrolysis of the lipid is optimal at pH 5.4 in acetate buffer. The reaction is stimulated by calcium ions or by high concentration of monovalent cations and, to a less extent, by long-chain cationic amphipathic compounds. Enzyme activity is lost on dialysis of the brain extract and can be restored by diffusible factor(s). Some differences in the conditions for hydrolysis of mono- and tri-phosphoinositides are noted.

scholarly journals Constancy of the optimum temperature of an enzyme under varying concentrations of substrate and of enzyme

1914 ◽  
Vol 88 (602) ◽  
pp. 258-262
Keyword(s):  
Experimental Evidence ◽  
Aspergillus Oryzae ◽  
Hydrolytic Enzyme ◽  
Fixed Duration ◽  
Optimum Temperature ◽  
Enzymic Hydrolysis ◽  
Main Interest ◽  
General Law ◽  
The Moment ◽  
Hydrolysis Of

In a recent paper a new enzymic relation is recorded. For the enzymic hydrolysis of salicin—by the enzyme which Gabriel Bertrand and the author have named salicinase —it is found that, in an action of fixed duration, the temperature of greatest activity of the ferment is always the same, whatever the dilutions of substrate and of enzyme adopted for the determination. In other words, the duration of the action being constant, the optimum tem­perature of the ferment is independent of the concentration both of the substrate and of the enzyme. The observation is suggestive: if true of one enzyme it may be true of all, and possibly becomes the enunciation of a general law. Herein, for the moment, lies its main interest. In the present paper further experimental evidence for this hypothesis in given, in the case of another hydrolytic enzyme, the maltase of Aspergillus oryzæ (taka-diastase).

scholarly journals Extracellular α-Galactosidase from Trichoderma sp. (WF-3): Optimization of Enzyme Production and Biochemical Characterization

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Aishwarya Singh Chauhan ◽  
Arunesh Kumar ◽  
Nikhat J. Siddiqi ◽  
B. Sharma
Keyword(s):  
Enzyme Activity ◽  
Enzyme Assay ◽  
Biochemical Characterization ◽  
Catalytic Efficiency ◽  
Culture Conditions ◽  
Significant Loss ◽  
Trichoderma Sp ◽  
Rate Of Reaction ◽  
Higher Temperature ◽  
Substrate Concentrations

Trichoderma spp. have been reported earlier for their excellent capacity of secreting extracellular α-galactosidase. This communication focuses on the optimization of culture conditions for optimal production of enzyme and its characterization. The evaluation of the effects of different enzyme assay parameters such as stability, pH, temperature, substrate concentrations, and incubation time on enzyme activity has been made. The most suitable buffer for enzyme assay was found to be citrate phosphate buffer (50 mM, pH 6.0) for optimal enzyme activity. This enzyme was fairly stable at higher temperature as it exhibited 72% activity at 60°C. The enzyme when incubated at room temperature up to two hours did not show any significant loss in activity. It followed Michaelis-Menten curve and showed direct relationship with varying substrate concentrations. Higher substrate concentration was not inhibitory to enzyme activity. The apparent Michaelis-Menten constant (Km), maximum rate of reaction (Vmax), Kcat, and catalytic efficiency values for this enzyme were calculated from the Lineweaver-Burk double reciprocal plot and were found to be 0.5 mM, 10 mM/s, 1.30 U mg−1, and 2.33 U mg−1 mM−1, respectively. This information would be helpful in understanding the biophysical and biochemical characteristics of extracellular α-galactosidase from other microbial sources.

scholarly journals Cover Feature: Distance between Metal Centres Affects Catalytic Efficiency of Dinuclear CoIII Complexes in the Hydrolysis of a Phosphate Diester (Eur. J. Org. Chem. 39/2018)

2018 ◽  
Vol 2018 (39) ◽  
pp. 5335-5335
Author(s):  
Eva Szusanna Bencze ◽  
Cristiano Zonta ◽  
Fabrizio Mancin ◽  
Leonard J. Prins ◽  
Paolo Scrimin
Keyword(s):  
Catalytic Efficiency ◽  
Phosphate Diester ◽  
Hydrolysis Of

scholarly journals Properties of a new fungal b-galactosidase with potential application in the dairy industry

1999 ◽  
Vol 30 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Rubens Cruz ◽  
Vinícius D'Arcádia Cruz ◽  
Juliana Gisele Belote ◽  
Marcelo de Oliveira Khenayfes ◽  
Claudia Dorta ◽  
...  
Keyword(s):  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Transferase Activity ◽  
Optimum Temperature ◽  
Milk Whey ◽  
Beneficial Effects ◽  
Optimum Ph ◽  
Semi Solid ◽  
Good Productivity ◽  
Hydrolysis Of

<FONT FACE="Symbol">b</font>-Galactosidase or <FONT FACE="Symbol">b</font>-D-galactoside-galactohydrolase (EC. 3.2.1.23) is an important enzyme industrially used for the hydrolysis of lactose from milk and milk whey for several applications. Lately, the importance of this enzyme was enhanced by its galactosyltransferase activity, which is responsible for the synthesis of transgalactosylated oligosaccharides (TOS) that act as functional foods, with several beneficial effects on consumers. Penicillium simplicissimum, a strain isolated from soil, when grown in semi-solid medium showed good productivity of <FONT FACE="Symbol">b</font>-galactosidase with galactosyltransferase activity. The optimum pH for hydrolysis was in the 4.04.6 range and the optimum pH for galactosyltransferase activity was in the 6.07.0 range. The optimum temperature for hydrolysis and transferase activity was 55-60°C and 50°C, respectively, and the enzyme showed high thermostability for the hydrolytic activity. The enzyme showed a potential for several industrial applications such as removal of 67% of the lactose from milk and 84% of the lactose from milk whey when incubated at their original pH (4.5 and 6.34, respectively) under optimum temperature conditions. When incubated with a 40% lactose solution in 150 mM McIlvaine buffer, pH 4.5, at 55°C the enzyme converted 86.5% of the lactose to its component monosaccharides. When incubated with a 60% lactose solution in the same buffer but at pH 6.5 and 50°C, the enzyme can synthetize up to 30.5% TOS, with 39.5% lactose and 30% monosaccharides remaining in the preparation.

scholarly journals Efficient Production of Acetic Acid from Nipa (Nypa fruticans) Sap by Moorella thermoacetica (f. Clostridium thermoaceticum)

2019 ◽  
Author(s):  
Dung Van Nguyen ◽  
Pinthep Sethapokin ◽  
Harifara Rabemanolontsoa ◽  
Eiji Minami ◽  
Haruo Kawamoto ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Oxalic Acid ◽  
Acid Catalyst ◽  
Cost Effective ◽  
Efficient Production ◽  
Acid Fermentation ◽  
Acid Yield ◽  
Moorella Thermoacetica ◽  
Nypa Fruticans ◽  
Hydrolysis Of

To valorize the underutilized nipa sap composed mainly of sucrose, glucose and fructose, acetic acid fermentation by Moorella thermoacetica was explored. Given that M. thermoacetica cannot directly metabolize sucrose, we evaluated various catalysts for the hydrolysis of this material. Oxalic acid and invertase exhibited high levels of activity towards the hydrolysis of the sucrose in nipa sap to glucose and fructose. Although these two methods consumed similar levels of energy for the hydrolysis of sucrose, oxalic acid was found to be more cost-effective. Nipa saps hydrolyzed by these two catalysts were also fermented by M. thermoacetica. The results revealed that the two hydrolyzed sap mixtures gave 10.0 g/L of acetic acid from the 10.2 g/L of substrate sugars in nipa sap. Notably, the results showed that the oxalic acid catalyst was also fermented to acetic acid, which avoided the need to remove the catalyst from the product stream. Taken together, these results show that oxalic acid hydrolysis is superior to enzymatic hydrolysis for the pretreatment of nipa sap. The acetic acid yield achieved in this study corresponds to a conversion efficiency of 98%, which is about 3.6 times higher than that achieved using the traditional methods. The process developed in this study therefore has high potential as a green biorefinery process for the efficient conversion of sucrose-containing nipa sap to bio-derived acetic acid.

Digestion in Ascidians and the Influence of Temperature

1929 ◽  
Vol 6 (3) ◽  
pp. 275-292
Author(s):  
N. J. BERRILL
Keyword(s):  
Enzyme Activity ◽  
Body Temperature ◽  
Digestive Enzymes ◽  
Alimentary Canal ◽  
The Body ◽  
Maximum Efficiency ◽  
Bile Pigment ◽  
Optimum Temperature ◽  
Different Temperatures ◽  
Pass Through

1. The mechanism of feeding and digestion in the Pyurid Ascidians Tethyum pyriforme americanum and Boltenia ovifera is described. 2. The structure and histology of the "liver" is described and it is shown that it is primarily an organ of secretion. 3. It is found that the only digestive enzymes are those poured into the gut by the liver, and consist of a powerful amylase, a protease, a very weak lipase, and also an invertase, a maltase, and a lactase. 4. The brownish pigment of the liver gives reactions with acids somewhat like those of bile pigment. There is no trace of bile salts, however, nor of cholesterol. 5. The amylase has an activity range from pH 6.0 topic pH 8.5 with an optimum near pH 7.5. The protease is active from pH 6.0 to above pH 10.0. A similar protease is secreted by Molgula citrina and Ascidia prunum. 6. The relative strengths of the amylase and protease are compared, the amylase being very much the stronger. 7. While experiments of brief duration indicate an optimum temperature for enzyme activity above 40° C, the more prolonged the experiments the lower does the optimum become. Whatever the optimum may be after an experiment of 2 hours' duration, it falls about 20° C. during the next 45 hours, if the experiments be so prolonged. 8. At 15° C. and at 10° C. the food takes about 35 and 55 hours respectively to pass through the alimentary canal, and at 50 C. somewhere between 70 and 90 hours. These temperatures approximately cover the normal range in temperature of the environment, and therefore of the animal itself. 9. From experiments lasting 33 hours the optimum temperature for enzyme activity was found to be about 17° C.; that is, within one or two degrees of the body temperature. From experiments lasting 57 hours the optimum temperature was found to be about 13° C ; that is, within three degrees of the body temperature. 10. These temperature optima not only represent the relative amounts of substrate converted at different temperatures, but also represent the absolute amounts converted and convertible. 11. The enzymes, amylase and protease, are two-thirds to three-quarters destroyed during their period of activity within the alimentary canal of the animal, and in order to utilise the remainder the digestion mixture would have to be retained within the canal for twice as long a time. 12. Therefore it seems probable that the organism in making such a compromise between a high activity of the enzyme and its economical use is working to a maximum efficiency; and it is possible that a permanent increase in the stability of the digestive enzymes would be turned to advantage through a more prolonged retention of the food within the gut.

The Efficient Production of High DP Chito-Oligosaccharides by Enzymatic Hydrolysis of Chitosan

1992 ◽  
pp. 259-267
Author(s):  
Etsudo Murakami ◽  
Kaname Hasegawa ◽  
Jun-Ichi Tamura ◽  
Kiyoshi Kadowaki
Keyword(s):  
Enzymatic Hydrolysis ◽  
Efficient Production ◽  
Hydrolysis Of
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