scholarly journals The Effect of Substrate Concentration on the Hydrolysis of Starch by the Amylase of Germinated Barley

1926 ◽  
Vol 20 (5) ◽  
pp. 1016-1023 ◽  
Author(s):  
George Sharp Eadie
Keyword(s):  
Substrate Concentration ◽  
Germinated Barley ◽  
Hydrolysis Of

scholarly journals The behaviour of trypsin towards α-N-methyl-α-N-toluene-p-sulphonyl-l-lysine β-naphthyl ester. A new method for determining the absolute molarity of solutions of trypsin

1968 ◽  
Vol 107 (1) ◽  
pp. 97-102 ◽  
Author(s):  
D. T. Elmore ◽  
J. J. Smyth
Keyword(s):  
Methyl Ester ◽  
Convenient Method ◽  
Substrate Concentration ◽  
Competitive Inhibitor ◽  
New Method ◽  
Spectrophotometric Measurement ◽  
Bovine Thrombin ◽  
The Absolute ◽  
Hydrolysis Of

1. α-N-Methyl-α-N-toluene-p-sulphonyl-l-lysine β-naphthyl ester (MTLNE) was synthesized as its hydrobromide and shown to be slowly hydrolysed by bovine pancreatic trypsin. The acylation step, however, is so much faster than deacylation of the acyl-enzyme that spectrophotometric measurement of the ‘burst’ of β-naphthol provides a convenient method for determining the absolute molarity of trypsin solutions. 2. By using the same stock solution of trypsin, application of this method at pH4·0 and pH7·0 as well as that of Bender et al. (1966) at pH3·7 gave concordant results. 3. Provided that [S]0>[E]0, the size of the ‘burst’ is independent of substrate concentration. 4. In the trypsin-catalysed hydrolysis of α-N-toluene-p-sulphonyl-l-arginine methyl ester, MTLNE functions as a powerful non-competitive inhibitor. 5. There is no detectable reaction between MTLNE and either bovine pancreatic α-chymotrypsin at pH4·0 or bovine thrombin at pH6·0.

scholarly journals Substrate Inhibition in the Hydrolysis of Hippuric Acid Esters by Carboxypeptidase A

1975 ◽  
Vol 53 (2) ◽  
pp. 283-294 ◽  
Author(s):  
Joe Murphy ◽  
John W. Bunting
Keyword(s):  
Substrate Concentration ◽  
Hippuric Acid ◽  
Substrate Inhibition ◽  
Competitive Inhibitor ◽  
Side Chain ◽  
Carboxypeptidase A ◽  
Substrate Activation ◽  
Hydrolysis Of ◽  
Substrate Concentrations ◽  
Acid Esters

The dependence of initial velocity upon substrate concentration has been examined in the carboxypeptidase A catalyzed hydrolysis of the following hippuric acid esters (at pH 7.5, 25°, ionic strength O.5): C6H5CONHCH2CO2CHRCO2H: R=CH3; CH2CH3;(CH2)2CH3; (CH2)3CH3; (CH2)5CH3; CH(CH3)2; CH2CH(CH3)2; C6H5; CH2C6H5. All of these esters display marked substrate inhibition of their enzymic hydrolyses. With the exception of R=CH3, the velocity-substrate concentration profiles for each of these esters can be rationalized by the formation of an E.S2 complex which, independent of the alcohol moiety of the ester, reacts approximately 25 times more slowly than the E.S complex. For most of these esters, the formation of E.S2 approximates ordered binding of the substrate molecules at the catalytic and inhibitory sites. While binding at the catalytic site is markedly dependent on the nature of the R group, binding of a second substrate molecule to E.S is not significantly affected by the nature of the R side chain. For R=C6H5, the D ester is neither a substrate nor a competitive inhibitor of the hydrolysis of the L-ester but can replace the L-ester at the binding site which is responsible for substrate inhibition. The kinetic analysis suggests that this behavior of D and L -enantiomers is also typical of the other esters examined (except possibly R=CH3). For R=CH3 only, substrate activation also seems to occur prior to the onset of substrate inhibition at higher substrate concentrations.

scholarly journals Optimisation of the Enzymatic Hydrolysis of Blood Cells with a Neutral Protease

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Yanbin Zheng ◽  
Qiushi Chen ◽  
Anshan Shan ◽  
Hao Zhang
Keyword(s):  
Amino Acids ◽  
Enzymatic Hydrolysis ◽  
Incubation Period ◽  
Blood Cells ◽  
Substrate Concentration ◽  
Neutral Protease ◽  
Degree Of Hydrolysis ◽  
Hydrolysis Conditions ◽  
Optimized Conditions ◽  
Hydrolysis Of

For utilizing the blood cells (BCs) effectively, enzymatic hydrolysis was applied to produce the enzymatically hydrolyzed blood cells (EHBCs) by using a neutral protease as a catalyst. The results of the single-factor experiments showed optimal substrate concentration, enzyme to substrate ratio (E/S), pH, temperature, and incubation period were 1.00%, 0.10, 7.00, 50.00°C, and 12.00 h, respectively. The optimized hydrolysis conditions from response surface methodology (RSM) were pH 6.50, E/S 0.11, temperature 45.00°C, and incubation period 12.00 h. Under these conditions (substrate concentration 1.00%), the degree of hydrolysis (DH) was 35.06%. The free amino acids (FAAs) content of the EHBCs (35.24%) was 40.46 times higher than BCs while the total amino acids (TAAs) content was lower than BCs. The scores of lysine (human 0.87; pig 0.97), valine (human 1.42; pig 1.38), leucine (human 1.50; pig 1.90), tyrosine (human 0.84; pig 1.09), and histidine (human 2.17; pig 2.50) indicated that the EHBCs basically fulfilled the adult human and pig nutritional requirements. The calculated protein efficiency ratios (C-PERs) of the EHBCs were 3.94, 6.19, 21.73, and 2.04. In summary, the EHBCs were produced successfully with optimized conditions and could be a novel protein source for humans and pigs.

scholarly journals DOES THE KINETICS OF TRYPSIN DIGESTION DEPEND ON THE FORMATION OF A COMPOUND BETWEEN ENZYME AND SUBSTRATE

1922 ◽  
Vol 4 (5) ◽  
pp. 487-509 ◽  
Author(s):  
John H. Northrop
Keyword(s):  
Experimental Evidence ◽  
Substrate Concentration ◽  
Relative Velocity ◽  
Mass Action ◽  
Law Of Mass Action ◽  
Rate Of Hydrolysis ◽  
Gelatin Concentration ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Substrate Concentrations

1. The velocity of hydrolysis of gelatin by trypsin increases more slowly than the gelatin concentration and finally becomes nearly independent of the gelatin concentration. The relative velocity of hydrolysis of any two substrate concentrations is independent of the quantity of enzyme used to make the comparison. 2. The rate of hydrolysis is independent of the viscosity of the solution. 3. The percentage retardation of the rate of hydrolysis by inhibiting substances, is independent of the substrate concentration. 4. There is experimental evidence that the enzyme and inhibiting substance are combined to form a widely dissociated compound. 5. If the substrate were also combined with the enzyme, an increase in the substrate concentration should affect the equilibrium between the enzyme and the inhibiting substance. This is not the case. 6. The rate of digestion of a mixture of casein and gelatin is equal to the sum of the rates of hydrolysis of the two substances alone, as it should be if the rate is proportional to the concentration of free enzyme. This contradicts the saturation hypothesis. 7. If the reaction is followed by determining directly the change in the substrate concentration, it is found that this change agrees with the law of mass action; i.e., the rate of digestion is proportional to the substrate concentration.

scholarly journals The Development of a Sorghum Bran-Based Biorefining Process to Convert Sorghum Bran into Value Added Products

Foods ◽  
2019 ◽  
Vol 8 (8) ◽  
pp. 279 ◽  
Author(s):  
Oyenike Makanjuola ◽  
Darren Greetham ◽  
Xiaoyan Zou ◽  
Chenyu Du
Keyword(s):  
Substrate Concentration ◽  
Large Scale ◽  
Value Added ◽  
Aspergillus Awamori ◽  
Glucoamylase Activity ◽  
Sorghum Bran ◽  
Loading Ratio ◽  
Food Processing Waste ◽  
Fermentation Parameters ◽  
Hydrolysis Of

Sorghum bran, a starch rich food processing waste, was investigated for the production of glucoamylase in submerged fungal fermentation using Aspergillus awamori. The fermentation parameters, such as cultivation time, substrate concentration, pH, temperature, nitrogen source, mineral source and the medium loading ratio were investigated. The glucoamylase activity was improved from 1.90 U/mL in an initial test, to 19.3 U/mL at 10% (w/v) substrate concentration, pH 6.0, medium loading ratio of 200 mL in 500 mL shaking flask, with the addition of 2.5 g/L yeast extract and essential minerals. Fermentation using 2 L bioreactors under the optimum conditions resulted in a glucoamylase activity of 23.5 U/mL at 72 h, while further increase in sorghum bran concentration to 12.5% (w/v) gave an improved gluco-amylase activity of 37.6 U/mL at 115 h. The crude glucoamylase solution was used for the enzymatic hydrolysis of the sorghum bran. A sorghum bran hydrolysis carried out at 200 rpm, 55 °C for 48 h at a substrate loading ratio of 80 g/L resulted in 11.7 g/L glucose, similar to the results obtained using commercial glucoamylase. Large-scale sorghum bran hydrolysis in 2 L bioreactors using crude glucoamylase solution resulted in a glucose concentration of 38.7 g/L from 200 g/L sorghum bran, corresponding to 94.1% of the theoretical hydrolysis yield.

scholarly journals THE KINETICS OF TRYPSIN DIGESTION

1924 ◽  
Vol 6 (4) ◽  
pp. 429-437 ◽  
Author(s):  
John H. Northrop
Keyword(s):  
High Temperature ◽  
Substrate Concentration ◽  
Trypsin Digestion ◽  
Velocity Constant ◽  
Rate Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of

1. A study has been made of the rate of hydrolysis of concentrated gelatin solutions at a high temperature and with a large amount of trypsin. 2. Under these conditions the substrate concentration may be considered constant and the only variable is the decrease in the amount of trypsin owing to inactivation. 3. The theory based on the mass law predicts that under these conditions (a) the rate at any time will be proportional to the concentration of trypsin at that time; (b) the reaction should approximate a monomolecular one if the total hydrolysis observed is taken as the amount of substrate available; (c) that the velocity constant calculated in this way should agree with the constant for the decomposition of the enzyme and that it should be independent of the concentration of enzyme instead of proportional to it as is usually the case; and (d) that the total amount of substrate decomposed should be proportional to the amount of trypsin added at the beginning instead of independent of it. These results have been obtained experimentally.

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