Defatted corn protein was digested using five different proteases, Alcalase, Trypsin, Neutrase, Protamex and Flavourzyme, in order to produce bile acid binding peptides. Bile acid binding capacity was analyzed in vitro using peptides from different proteases of defatted corn hydrolysate. Some crystalline bile acids like sodium glycocholate, sodium cholate and sodium deoxycholate were individually tested using HPLC to see which enzymes can release more peptides with high bile acid binding capacity. The bile acid binding capacity of Flavourzyme hydrolysate was almost preserved after gastrointestinal proteases digestion.
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The reac-tions were carried out for 10min in 0.
Theamount of enzyme added to the reaction solution was 0. Also, to deter-mine decay and product inhibition effects for Alcalase, a series of inhibition experi-ments were conducted with the addition of various amounts of hydrolysate.
For eachexperimental run, both the amount of hydrolysis meqv L1 and the soluble proteinamount g L1 were investigated with respect to time, and the initial reaction rateswere determined from the slopes of the linear models that fitted to these experi-mental data.
The kinetic parameters, Km and Vmax were estimated as The type of inhibition for Alcalase was determined asuncompetitive, and the inhibition constant, Ki, was estimated as Keywords Alcalase; Corn gluten; Hydrolysis kinetics; Product inhibitionIntroductionProtein hydrolysis is carried out for many reasons, including improving nutritionalvalue, retarding deterioration, imparting texture, increasing solubility, adding foam-ing or coagulation properties, adding emulsifying capacity, preventing undesiredinteractions, removing off-flavors or odors, removing toxic or inhibitory ingredients,and isolation of bioactive peptides Lahl and Braun, ; Kim et al.
Traditionally, proteins are hydrolyzed by chemical means. However,hydrolysis by chemical reagents produces no selective by-products. The use ofenzymes provides milder process conditions and allows for a selective hydrolysisof protein Kim et al. New sources of food proteins are needed because ofincreasing global demand.
Hence, over the past decade, plant proteins as alternativesto animal proteins are increasingly being used since they are an economic and versa-tile substitute for animal proteins Friedman, ; Wang et al.
Corn gluten is a by-product from the production of starch from maize. For thisreason, knowledge of the kinetics of the reaction will be essential to optimize thehydrolysis process.
In the literature, the hydrolysis of corn gluten was performedby Kim et al. However, limited studies have been performed concerning thehydrolysis kinetics of corn gluten Mannheim and Cheryan, ; Hardwick andGlatz, On the other hand, enzyme inhibition is one of the constraints of thereactions catalyzed by the enzymes; hence, to optimize the process, information isrequired that describes the inhibition mechanisms that affect the process yield.
Therefore, aims of the present study are to investigate the reaction kinetics of corngluten hydrolysis and to determine decay and product inhibition effects for alcalase.
Materials and MethodsMaterialsCorn gluten used in this research, which contains The enzyme used in this work was Alcalase 2. MethodsThe reactions were monitored by using pH-stat method. The adjustment of pHduring hydrolysis was made with 0. The amount of hydrolysis wascalculated by Equation 1: The degree of dissociation of a-NH2 groups was computed from the followingequation: OzbekDownloaded by [University of Central Florida] at Prior to hydrolysis, thebackground protein of corn gluten and the protein concentration of enzyme werecalculated and subtracted from the overall protein.
For each sample, the assaywas carried out in triplicate and their averages were taken. Enzymatic HydrolysisHydrolysis experiments were carried out in a mL jacketed reactor with magneticstirring and automatic pH and temperature control.
A measured amount of corn gluten was added to the reactor containing mLof distilled water and allowed to disperse, and then the pH and temperature of thereaction solution were set.Disclosed herein are methods of making hydrolyzed proteins by enzymatic conversion.
The methods provide a process for producing enzyme hydrolyzed corn gluten meal. In some embodiments, the methods utilize a multistep process using various enzyme cocktails to produce corn gluten meal with improved degree of hydrolysis and solubility. The aim of this study was to investigate the influences of substrate concentration, enzyme concentration, temperature and pH on hydrolysis and solubilization of corn gluten as well as enzyme stability.
The corn gluten was hydrolyzed by. In the present study, the reaction kinetics of corn gluten hydrolysis by Alcalase, a bacterial protease produced by Bacillus licheniformis, was investigated. Corn gluten meal was hydrolyzed with Alcalase L, an alkaline protease.
The effects of enzyme concentration and gluten size reduction on the hydrolysis were studied. Before enzymatic hydrolysis, the zein suspension was maintained at 20, 30, 40 and 50 °C Next, alcalase (E/S = U/g) was added to start the reaction and the pH was kept at by continuously adding 1 M NaOH during the hydrolysis process.
The aim of this study was to investigate the influences of substrate concentration, enzyme concentration, temperature and pH on hydrolysis and solubilization of corn gluten as well as enzyme stability. The corn gluten was hydrolyzed by Alcalase enzyme (a bacterial protease produced by a selected.