Laurent Bazinet
Laval University
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Featured researches published by Laurent Bazinet.
Trends in Food Science and Technology | 1998
Laurent Bazinet; F Lamarche; D Ippersiel
Electrodialysis is an electrochemical process mainly used in industry for solution demineralization. A new type of membrane, the bipolar membrane, allows the electro-dissociation of water. The first industrial application of bipolar-membrane electrodialysis was oriented toward the recovery of acids and bases from salt streams. Recently, bipolar-membrane electrodialysis has been used to inhibit polyphenol oxidase in apple juice, the enzyme responsible for the enzymatic browning of cloudy juice, and to separate soybean proteins from other components without denaturing them, in order to produce protein isolates. Bipolar-membrane electrodialysis technology is an environmentally friendly technology with a wide-ranging application potential.
Critical Reviews in Food Science and Nutrition | 2005
Laurent Bazinet
Abstract Electrodialysis (ED) is an electrochemical separation process by which electrically-charged species are transported from one solution to another. ED is a combined method of dialysis and electrolysis and can be performed with two main cell types: multi-membrane cells for dilution-concentration and water dissociation applications (membrane phenomena), and electrolysis cells for redox reactions (electrode phenomena). The dilution-concentration principle applications in the dairy industry consist mainly of the demineralization of milk or milk by-products. The use of ED with monopolar membrane for protein separation and acid caseinate production, and in bioreactors for organic acid production, is also studied in the dairy industry. The interest of ED as a membrane process has been triggered recently by the development of a new membrane type, bipolar membrane. This membrane carries out the dissociation of water molecules. ED with bipolar membranes was applied very recently to the production of lactic acid from whey product fermentation, production of caseinates, and fractionation of whey proteins. Two principle applications of electrode reactions were published: electrochemical coagulation (EC) to precipitate milk proteins, and electroreduction for the reduction of disulfide bonds in the proteins. It appears in this article that processes using membrane phenomena are more numerous and developed than electrolytic applications. This is the composition of milk and the lack of knowledge of redox reactions of the different food compounds that limit the applications and the development of electrolytic phenomena. Electrodialytic phenomena present a great potential for application in the dairy industry, and more generally, in the food industry; many of these applications have to be discovered.
Advances in Colloid and Interface Science | 2016
Sergey Mikhaylin; Laurent Bazinet
The environmentally friendly ion-exchange membrane (IEM) processes find more and more applications in the modern industries in order to demineralize, concentrate and modify products. Moreover, these processes may be applied for the energy conversion and storage. However, the main drawback of the IEM processes is a formation of fouling, which significantly decreases the process efficiency and increases the process cost. The present review is dedicated to the problematic of IEM fouling phenomena. Firstly, the major types of IEM fouling such as colloidal fouling, organic fouling, scaling and biofouling are discussed along with consideration of the main factors affecting fouling formation and development. Secondly, the review of the possible methods of IEM fouling characterization is provided. This section includes the methods of fouling visualization and characterization as well as methods allowing investigations of characteristics of the fouled IEMs. Eventually, the reader will find the conventional and modern strategies of prevention and control of different fouling types.
Food Chemistry | 2014
Alain Doyen; Chibuike C. Udenigwe; Patricia L. Mitchell; André Marette; Rotimi E. Aluko; Laurent Bazinet
Flaxseed protein hydrolysate has been fractionated by electrodialysis with two ultrafiltration membranes (20 and 50 kDa) stacked in the system for the recovery of two specific cationic peptide fractions (KCl-F1 and KCl-F2). After 360 min of treatment, peptide migration increased as a function of time in KCl compartments. Moreover, the use of two different ultrafiltration membrane allowed concentration of the 300-400 and 400-500 Da molecular weight range peptides in the KCl-F1 and KCl-F2 fractions, respectively, compared to the initial hydrolysate. After mass spectrometry analysis, higher amounts of low molecular weight peptides were recovered in the KCl-F2 compartment while relatively higher molecular weight peptides were more detected in the KCl-F1 compartment. Amino acid analysis showed that His, Lys and Arg were especially concentrated in the KCl compartments. Finally, glucose-transport assay demonstrated that the KCl-F2 fraction increased glucose uptake while oral administration of KCl-F1 and final FPH decreased systolic blood pressure.
Journal of Chromatography A | 2008
Frantz Le Dévédec; Laurent Bazinet; Alexandra Furtos; Karine Venne; Serge Brunet; Mircea Alexandru Mateescu
A novel approach for chitosan oligosaccharide (COS) separation by immobilized metal affinity chromatography (IMAC) based on the differences in the interactions of chelated copper (II) ions with various COS (dimers, trimers, tetramers) is described. Polyhydroxylic chromatographic supports (agarose CL-6B and silica) were functionalized with various chelating functions such as iminodiacetate (IDA), carboxymethyl-aspartate (CM-Asp) and tris(carboxymethyl)ethylenediamine (TED). The COS retention capacities of the columns were between 2 and 6 mg/cm(3), depending on the chelating group. The COS were separated and/or enriched up to 95% for dimer and trimer and 90% for the tetramer, with yields of 60-95%.
Recent Patents on Biotechnology | 2009
Laurent Bazinet; Loubna Firdaous
In recent years, functional foods and nutraceuticals has attracted much attention, particularly for their impact on human health and prevention of certain diseases. Consequently, the production and properties of bioactive peptides has received an increasing scientific interest over the past few years. Considering that most functional peptides are present in complex matrices containing a large number of hydrolyzed protein fractions, their separation and purification are required. Conventional pressure-driven processes can be used for amino acids and peptides separation but are limited by their fouling problems and their low selectivity when separating similar sized biomolecules. To improve the separation efficiency, an external electric field was applied during pressure-driven filtration. However, the pressure gradient brings about the accumulation of peptides at the nearby membrane surface and affects the membrane transport selectivity. Processes combining an electrical field as a driving force to porous membranes have been developed for the separation of biopeptides to obtain better purified products. Compounds of higher molecular weights than the membrane cut-off can be separated. The first trials were carried-out to perform the separation of amino acids and peptides with a filtration module specially designed and using one ultrafiltration membrane. More recently, electrodialysis with ultrafiltration membranes has been developed to fractionate simultaneously acidic and basic peptides, using a conventional electrodialysis cell, in which some ion exchange membranes are replaced by ultrafiltration ones. The perspectives in this field will be the understanding of the interactions of peptides and membrane as well as the development of new membrane materials limitating or increasing these interactions to improve the selectivity and the yield of production of specific peptides. This review article also discusses recent patents related to bioactive peptides.
Food Chemistry | 2012
Chibuike C. Udenigwe; Abayomi P. Adebiyi; Alain Doyen; Huan Li; Laurent Bazinet; Rotimi E. Aluko
Flaxseed protein isolate (FPI) contains high amount of arginine, which plays important physiological roles especially as nitric oxide precursor in the vascular endothelium. Arginine-rich peptides can be generated from FPI and used as a source of nitric oxide, which can produce in vivo vasodilatory effects during hypertension. Enzymatic hydrolysis of FPI with trypsin and pronase resulted in a hydrolysate that was fractionated using electrodialysis-ultrafiltration (EDUF). EDUF experiment resulted in migration of peptides to the anionic and cationic recovery compartments. Compared to FPI with 11% arginine, about one-third of the cationic fraction was composed of arginine. Thirteen potential peptide sequences were identified to be present in the cationic compartment of which 12 contained at least one arginine residue. None of the peptides identified from the anionic compartment contained arginine. Oral administration of the cationic peptides (200mg/kgbodywt.) to spontaneously hypertensive rats resulted in a more rapid decrease in systolic blood pressure when compared to similar amounts of FPI or the amino acid form of arginine. It was concluded that the rapid effect of the arginine-rich peptide product suggests faster rate of peptide absorption than amino acids and this may be exploited to provide fast relief from hypertension.
RSC Advances | 2015
Aishwarya Mohan; Subin R. C. K. Rajendran; Quan Sophia He; Laurent Bazinet; Chibuike C. Udenigwe
Food protein hydrolysates and peptides are considered a category of promising functional food ingredients. However, commercial application of protein hydrolysates and their constituent peptides can be impeded by their low bioavailability, bitter taste, hygroscopicity and likelihood of interacting with the food matrix. Encapsulation as a delivery mechanism can be used to overcome these challenges for improving the bioavailability and organoleptic properties of the peptides. Proteins, polysaccharides and lipids are the three carrier systems that have been utilized in food peptide encapsulation. The protein and polysaccharide systems mainly aim at masking the bitter taste and reducing the hygroscopicity of protein hydrolysates, whereas the lipid-based systems are intended for use in enhancing the bioavailability and biostability of encapsulated peptides. A spray drying technique is largely used to achieve microencapsulation in both protein and polysaccharide systems while, generally, liposomes are prepared by a film hydration technique. However, it is seen that the encapsulation efficiency (EE) of peptides using the liposome model is relatively lower since the entropy-driven liposome formation is uncontrolled and spontaneous. Achieving adequate EE through cost effective techniques is indispensable for encapsulation to be applicable to bioactive peptide-based product commercialization. Furthermore, the design of high quality functional foods requires detailed understanding of the release mechanism and kinetics, gastrointestinal stability, bioavailability and physiological bioactivity of the encapsulated peptide products.
Food Chemistry | 2012
Alain Doyen; Linda Saucier; Lucie Beaulieu; Yves Pouliot; Laurent Bazinet
Recently, a snow crab by-products hydrolysate has demonstrated antibacterial properties due to a peptide with a molecular weight of about 800Da, but only at high concentration. Consequently, peptide hydrolysate has been fractionated to obtain peptides in a more purified form. The aim of this work was to separate a snow crab by-products hydrolysate by electrodialysis with ultrafiltration membranes (EDUF). EDUF, which allows separation of molecules according to their charges and molecular weights, was used to recover and concentrate the active antibacterial fraction. Two different ultrafiltration membranes (20 and 50kDa) and two electrical field strengths (2 and 14V/cm) were used as separation parameters. After EDUF separation, the 300-600Da peptide molecular weight range was the most recovered with an abundance of 94%. Moreover, fractionation at 14V/cm with ultrafiltration membranes of 50kDa allowed the recovery of an anionic fraction which showed antibacterial properties on Escherichia coli ATCC 25922 and Listeria innocua HPB 13.
Journal of Agricultural and Food Chemistry | 2011
Alain Doyen; Lucie Beaulieu; Linda Saucier; Yves Pouliot; Laurent Bazinet
Electrodialysis with ultrafiltration membrane (EDUF) is a technology based on the separation of molecules according to their charge and molecular mass. Some works have already successfully demonstrated the recovery of bioactive peptide fractions. However, the impact of ultrafiltration membrane (UFM) material, used in the EDUF system, on the peptide migration has never been studied. Consequently, the objectives of this work were (1) to evaluate the effect of two different UFM materials on the selective separation of peptides from a snow crab byproduct hydrolysate by electrodialysis with ultrafiltration membranes and (2) to determine the effect of UFM material on their potential fouling by peptides. It appeared that, after 6 h of EDUF separation using polyether sulfone (PES) and cellulose acetate (CA) UFM, peptides with low molecular weights ranging from 300 to 700 Da represented the most abundant population in the KCl1 (compartment located near the anode for the recovery of anionic/acid peptide fractions) and KCl2 (compartment located near the cathode for the recovery of cationic/basic peptide fractions) permeates. Peptides with molecular weights ranging from 700 to 900 Da did not migrate during the EDUF treatment. Moreover, only CA UFM allowed the recovery of high molecular weight molecules (900-20000 Da) in both KCl compartments. Peptides desorbed from PES and CA UFM after 6 h of EDUF separation had low molecular weights and belonged mainly to the 600-700 Da molecular weight range. These peptides represented a low proportion of the peptides initially present in the snow crab byproduct hydrolysate with individual molecular weight range proportions from 1.52 ± 0.31 to 10.2 ± 2.32%.