Alcalase is the enzyme of choice to release antihypertensive peptides from amaranth proteins, but the hydrolysis conditions have not been optimized yet. Furthermore, in vivo assays are needed to confirm such a hypotensive effect. Our aim was to optimize the hydrolysis of amaranth protein with alcalase and to test in vivo the hypotensive effect of the hydrolysates. A response surface analysis wa...

The enzymatic hydrolysis of cellulose to glucose by cellulases is one of the major steps involved in the conversion of lignocellulosic biomass to yield biofuel. This hydrolysis by cellulases, a heterogeneous reaction, currently suffers from some major limitations, most importantly a dramatic rate slowdown at high degrees of conversion. To render the process economically viable, increases in hyd...

The administration of methenamine mandelate (Mandelamine) to pregnant women causes the levels of estriol in their urines to be unmeasurably low when acid hydrolysis is used. When enzyme hydrolysis replaces acid hydrolysis, normal estriol values are obtained. This result is attributed to the formaldehyde released by acid from hexamethylenetetramine, a constituent of the drug. The formaldehyde re...

Enzyme-substrate binding constants, K’e, for chymotrypsin and specific amide (N-acetyl-Mryptophanamide and Nacetyl-L-phenylalaninamide) and ester (N-acetyl-L-tryptophan ethyl ester) substrates have been measured by a proflavin-displacement method. Also, the rate constant for the formation of one intermediate in the chymotrypsincatalyzed hydrolysis of the ester has been determined at selected pH...

The phosphotriesterase from Pseudomonas diminuta was tested as a catalyst for the hydrolysis of phosphofluoridates. The purified enzyme has been shown to hydrolyze the phosphorus-fluorine bond of diisopropyl fluorophosphate, isopropyl methylphosphonofluoridate, and 1,2,2-trimethylpropylmethylphosphonofluoridate at pH 7.0, 25 degrees C, with turnover numbers of 41, 56, and 5 s-1, respectively. T...

The separation method and some properties of isodynamic acid phosphatases catalyzing FMN hydrolysis in spinach leaves were investigated. 1. The enzyme catalyzing FMN hydrolysis was found to occur practically and exclusively in the final supernatant fraction by differential centrifugation. 2. Acid phosphatase catalyzing FMN hydrolysis was separated into three fractions by chromatography on Sepha...

The kinetics of release of 4-nitrophenol were followed by stopped-flow spectrophotometry with two 4-nitrophenyl ester substrates of penicillin G acylase from Kluyvera citrophila. With the ester of acetic acid, but not of propionic acid, there was a pre-steady-state exponential phase, the kinetics of which were inhibited by phenylacetic acid (a product of hydrolysis of specific substrates) to th...

BACKGROUND Glycoside hydrolases (GHs) are enzymes that hydrolyze polysaccharides into simple sugars. To better understand the specificity of enzyme hydrolysis within the complex matrix of polysaccharides found in the plant cell wall, we studied the reactions of individual enzymes using glycome profiling, where a comprehensive collection of cell wall glycan-directed monoclonal antibodies are use...

AaCel9A [β-1,4-endoglucanase, (E.C:3.2.1.4)], was immobilized onto glutaraldehyde activated chitosan macrosphere by covalent attachment. The properties of the immobilized AaCel9A were investigated by determining the optimum pH and optimum temperature for activity, thermal stability, and kinetic parameters. The immobilization process shifted the enzyme’s optimum temperature from 65 °C for the fr...