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>

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 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.

Glycosidases in bovine milk: α-mannosidase and its inhibition by zwitterions

1968 ◽  
Vol 46 (11) ◽  
pp. 1351-1356 ◽  
Author(s):  
A. Mellors ◽  
V. R. Harwalkar
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Bovine Milk ◽  
Maximum Activity ◽  
Manganese Ions ◽  
Ammonium Sulfate Precipitation ◽  
Optimum Ph ◽  
High Concentrations ◽  
Hydrolysis Of ◽  
Dibasic Amino Acids

α-Mannosidase is present in bovine milk and is associated with the β-casein fraction following polyacrylamide gel electrophoresis. It was separated from the casein complex by ammonium sulfate precipitation in the presence of 10% (v/v) ethanol. Zinc or manganese ions are required for maximum activity and the enzyme is very labile. The optimum pH for the hydrolysis of p-nitrophenyl α-mannoside is about 3. In the presence of amino acid buffers the enzyme is inhibited. For dibasic amino acids this inhibition is inversely related to the [Formula: see text] of the amino acid and is apparently due to inhibition by zwitterions. High concentrations of the substrate p-nitrophenyl α-mannoside are inhibitory, and the apparent Km for this hydrolysis is 1.2 mM.

Muscle Arylamidase Activity of Several Marine Species

1974 ◽  
Vol 31 (4) ◽  
pp. 445-449
Author(s):  
Beverly A. Bauer ◽  
R. R. Eitenmiller
Keyword(s):  
Blue Crab ◽  
Gel Electrophoresis ◽  
Marine Species ◽  
Maximum Activity ◽  
Crude Extracts ◽  
Muscle Extract ◽  
Optimum Ph

Arylamidase activity in muscle extracts of mackerel, mullet, whiting, blue crab, quahog clam, and shrimp was investigated. The optimum pH for activity was between 7.0 and 7.5 for each species using alanyl-β-naphthylamide as substrate. Enzymes of the three species of fish exhibited maximum activity against alanyl-β-naphthylamide, whereas the clam showed maximum activity with leucyl-β-naphthylamide and the crab and shrimp with lysyl-β-naphthylamide. Puromycin inhibited each of the arylamidases. Acrylamide gel electrophoresis of the crude extracts suggested the presence of one arylamidase in muscle of the fish, crab, and clam. The shrimp muscle extract contained two active enzymes. Upon electrophoresis, the faster moving enzyme from shrimp muscle was active against lysyl-, alanyl-, and leucyl-β-naphthylamides, but the slower moving enzyme was active only against lysyl-β-naphthylamide.

scholarly journals Hydrolysis of penicillins and related compounds by the cell-bound penicillin acylase of Escherichia coli

1969 ◽  
Vol 115 (4) ◽  
pp. 733-739 ◽  
Author(s):  
M. Cole
Keyword(s):  
Escherichia Coli ◽  
Penicillin Acylase ◽  
Side Chain ◽  
Bacterial Cells ◽  
Optimum Temperature ◽  
Phenoxymethyl Penicillin ◽  
Optimum Ph ◽  
Penicillanic Acid ◽  
Hydrolysis Of ◽  
Related Compounds

1. A method is given for the preparation of penicillin acylase by using Escherichia coli N.C.I.B. 8743 and a strain selected for higher yield. The enzyme is associated with the bacterial cells and removes the side chains of penicillins to give 6-amino-penicillanic acid and a carboxylic acid. 2. The rates of penicillin deacylation indicated that p-hydroxybenzylpenicillin was the best substrate, followed in diminishing order by benzyl-, dl-α-hydroxybenzyl-, 2-furylmethyl-, 2-thienylmethyl-, d-α-aminobenzyl-, n-propoxymethyl- and isobutoxymethyl-penicillin. Phenylpenicillin and dl-α-carboxybenzylpenicillin were not substrates and phenoxymethyl-penicillin was very poor. 3. Amides and esters of the above penicillins were also substrates for the deacylation reaction, as were cephalosporins with a thienylmethyl side chain. 4. For the deacylation of 2-furylmethylpenicillin at 21° the optimum pH was 8·2. The optimum temperature was 60° at pH7. 5. By using selection A of N.C.I.B. 8743 and determining reaction velocities by assaying yields of 6-amino-penicillanic acid in a 10min. reaction at 50° and pH8·2, the Km for benzylpenicillin was found to be about 30mm and the Km for 2-furylmethylpenicillin, about 10mm. The Vmax. values were 0·6 and 0·24μmole/min./mg. of bacterial cells respectively.

Cinnamate-4-Hydroxyiase in Polyporus hispidus

1973 ◽  
Vol 51 (6) ◽  
pp. 731-734 ◽  
Author(s):  
C. P. Vance ◽  
A. M. D. Nambudiri ◽  
G. H. N. Towers
Keyword(s):  
Enzyme Activity ◽  
Enzymatic Activity ◽  
Microsomal Fraction ◽  
Mitochondrial Fraction ◽  
Maximum Activity ◽  
Coumaric Acid ◽  
Free System ◽  
Optimum Ph ◽  
A Cell ◽  
Plant Enzyme

A cell-free system capable of hydroxylating cinnamic acid to p-coumaric acid has been isolated from 10-day-oid cultures of Polyporus hispidus. The enzyme requires NADPH and FAD for maximum activity. Enzyme activity appears to be localized in the microsomal fraction with slight activity occurring in the mitochondrial fraction. The optimum pH for enzymatic activity is 7.5. This is the first report on any properties of this enzyme in a fungus. The enzyme differs from the known plant enzyme in its FAD requirement.

scholarly journals Isolation and caracterization of ficin enzyme from Ficus septica Burm F stem latex

2017 ◽  
Vol 20 (2) ◽  
pp. 161
Author(s):  
Sri Wahyuni ◽  
R. Susanti ◽  
Retno Sri Iswari
Keyword(s):  
Enzyme Activity ◽  
Column Chromatography ◽  
Temperature Treatment ◽  
Optimum Temperature ◽  
Optimum Ph ◽  
Incubation Temperatures ◽  
Joint Treatment ◽  
Plant Latex

This research aims to isolate and characterize the fcin enzyme from Ficus septica stem latex. Ficin from Ficus septica stem latex was isolated using column chromatography. Then enzyme activity was tested at different temperature (40oC, 50oC, 60oC, 70oC) and pH (6.0, 7.0, 8.0) levels. Ficin enzyme activity of joint treatment with variations in temperature and pH was analyzed using two-way ANOVA with a factorial pattern followed by Least Signifcant Difference (LSD) test. The results showed that temperature treatment signifcantly affects enzyme activity. However, the treatment of pH and the interaction between temperature and pH did not signifcantly affect the fcin enzyme activity. There was no signifcant difference in fcin activity at the incubation temperatures of 40oC and 50oC, as well as 60oC and 70oC. However, comparing the incubation temperatures of 40oC and 50oC with treatment 60°C and 70°C showed a signifcant difference in fcin enzyme activity. In the treatment of incubation at pH 6, 7 and 8 for fcin enzyme activity showed no signifcant difference. We concluded that the Ficus septica plant latex contained fcin enzyme with an optimum temperature of 60°C and optimum pH of 6, 7, and 8.

scholarly journals Purification and characterization of amylase from local isolate Pseudomonas sp.SPH4

2012 ◽  
Vol 6 (1) ◽  
pp. 69-79
Author(s):  
Hala M. Ali ◽  
Ghazi M. Aziz
Keyword(s):  
Enzyme Activity ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Silver Ions ◽  
Enzyme Characterization ◽  
Maximum Activity ◽  
Mercury Ions ◽  
Local Isolate ◽  
Optimum Ph

The amylase produced from local isolate Pseudomonas sp. SPH4 was purified by precipitation with 30% saturation ammonium sulphate, followed by ion-exchange chromotography using DEAE-cellulose column, and Gel filtration using Sephacryl S-300 column.The two iso-enzymes (a, b) were purified to (2.83, 3.47) times in the last step with an enzymes yields of (32.36, 76.34)% respectively. Enzyme characterization of the two iso-enzymes indicated that the optimum pH for the two iso-enzymes a and b were (7, 7.5) respectively, while the optimum pH for the iso-enzymes stability were (6.5, 7) respectively. The maximum activity for iso-enzymes (a, b) appeared at 45ºC and stable for 15 min at 30-50ºC and lost approximately 50% of it's activity at rang above 75ºC. Enzyme characterization results showed that the chlorides of silver and mercury had inhibitory effect on enzyme activity, the remaining enzyme activity for the iso-enzymes (a, b) were (46.66, 36.36)% for silver ions and (41.33, 33.63)% for mercury ions at 5 mM respectively, and (28, 28.18)% for silver ions and (25.33, 19.09)% for mercury ions at 10 mM respectively. The iso-enzymes a and b were affected by chelating agent ethylene diamine tetra acetic acid (EDTA) at concentration 2mM the remaining activity (45.33, 43.63)% respectively, and 5mM the remaining activity (28, 28.18)% respectivily, and these iso-enzymes (a, b) refered to metalloenzymes. The iso-enzymes (a, b) were kept their activity when treated by reducing agent (2-mercaptoethanol) at 2 mM the remaining activity (92, 92.72)% respectively, and 5 mM the remaining activity (85.3, 89.09)% respectivily. The iso-enzymes (a, b) were kept their activity when treated by phenyl methyl sulphonyl fluoride (PMSF) at concentration 1mM the remaining activity (93.33, 90.90)% respectivily,and 5 mM the remaining activity (90.66, 87.27)% respectivily, and these indicated that these iso-enzymes didnot referred to serineamylases group.

scholarly journals Influence of pH, Temperature and Various Heavy Metals on β-galactosidase Activity in the Crude Extract of Pleurotus ostreatus

2017 ◽  
Vol 5 (1) ◽  
pp. 29
Author(s):  
Tariq H. Shloul ◽  
Omar M. Atrooz ◽  
Mohammad H. Abukhalil
Keyword(s):  
Heavy Metals ◽  
Crude Extract ◽  
Pleurotus Ostreatus ◽  
Competitive Inhibition ◽  
Maximum Activity ◽  
Galactosidase Activity ◽  
Crude Extracts ◽  
Influence Of Ph ◽  
Hydrolysis Of

The aim of this study was to determine the activity of β-galactosidase in the crude extracts of Pleurotus ostreatus in the presence and absence of various heavy metals. β-galactosidase (EC 3.2.1.23), is a hydrolase enzyme which helps in the hydrolysis of lactose into monosaccharides. Characterization of β-galactosidase from Pleurotus ostreatus was achieved using the substrate 2-nitrophenyl β-D-galactopyranoside (ONPG). The pH and temperature profiles of β-galactosidase showed maximum activity at pH 3.0 and at 50°C, respectively. The Vmax  and Km values of β-galactosidase using ONPG as a substrate was found to be 0.571 μmol/min and 0.307 mM, respectively. These results revealed that the β-galactosidase activity in the crude extracts of Pleurotus ostreatus was changed in the presence of different heavy metals. The results indicated that Hg2+ and Mo2+ have an uncompetitive inhibition on the β- galactosidase activity in the extract of Pleurotus ostreatus by decreasing both Km and Vmax values.  while Al3+, Cu2+, Cr3+, Zn2+ and Ni2+  showed mixed inhibition  activity  by decreasing Vmax values and  by increasing Km values. However, Pb2+ was found to act as a non-competitive inhibition by decreasing Vmax value. The findings suggested that crude extract of Pleurotus ostreatus can be used as a source of β-galactosidase for medical and industrial purposes.

Preparation of Genipin by Hydrolysis of Geniposide with Co-Immobilized Enzyme

2011 ◽  
Vol 236-238 ◽  
pp. 1793-1798 ◽  
Author(s):  
Hua Zheng Liang ◽  
He Chen ◽  
Jian Feng Wang ◽  
Yu Lan He
Keyword(s):  
High Performance ◽  
Immobilized Enzyme ◽  
Low Cost ◽  
Enzymatic Properties ◽  
High Yield ◽  
Cross Linking ◽  
Optimum Temperature ◽  
Environmental Friendly ◽  
Optimum Ph ◽  
Hydrolysis Of

Co-immobilize enzyme by cross-linking and embedding, optimize conditions for immobilizing, determinate the enzymatic properties of co-immobilized enzyme and study the methods for preparation of genipin using co-immobilized enzyme to hydrolyze geniposide. Optimized immobilizing conditions include glutaraldehyde concentration being 0.15%, cross-linking temperature being 20°C, cross-linking time being 2 hours, the activity of co-immobilized β-glucosidase and cell reaches to 65.33U/mg and the enzyme activity recovery being 52.63%. Enzymatic properties of co-immobilized enzyme are following: optimum temperature is 55°C and optimum pH is 5.0. The transformation experiments are carried out with co-immobilized enzyme. The results show that half-life of co-immobilized enzyme reaches around 40 days, higher than the normal immobilized enzyme. The conversion rate of geniposide is above 95% after 8 hours. The genipin is isolated, purified and recrystallized to reach more than 98% of purity by High Performance Liquid Chromatography. Advantages to prepare genipin using co-immobilized enzyme include low cost, high yield, environmental friendly and easy to manufacturing.

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