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Dive into the research topics where Michael T. Nickerson is active.

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Featured researches published by Michael T. Nickerson.


Food Chemistry | 2013

Food proteins: A review on their emulsifying properties using a structure-function approach

Ricky S.H. Lam; Michael T. Nickerson

Proteins are of great interest due to their amphiphilic nature, which allows them to reduce the interfacial tension at the oil-water interface. The incorporation of proteins at the oil-water interface has allowed scientists to utilise them to form emulsions (O/W or W/O), which may be used in food formulations, drug and nutrient delivery. The systematic study of the proteins at the interface and the factors that affect their stability (i.e., conformation, pH, solvent conditions, and thermal treatment) has allowed for a broader use of these emulsions tailored for various applications. In this review, the factors affecting the stability of emulsions using food proteins will be discussed. The use of polysaccharides to complex with proteins will also be explored in relation to enhancing emulsion stability.


Journal of Agricultural and Food Chemistry | 2009

Effect of pH, Salt, and Biopolymer Ratio on the Formation of Pea Protein Isolate−Gum Arabic Complexes

Shuanghui Liu; Nicholas H. Low; Michael T. Nickerson

Turbidity measurements were used to study the formation of soluble and insoluble complexes between pea protein isolate (PPI) and gum arabic (GA) mixtures as a function of pH (6.0-1.5), salt concentration (NaCl, 0-50 mM), and protein-polysaccharide weight mixing ratio (1:4 to 10:1 w/w). For mixtures in the absence of salt and at a 1:1 mixing ratio, two structure-forming transitions were observed as a function of pH. The first event occurred at a pH of 4.2, with the second at pH 3.7, indicating the formation of soluble and insoluble complexes, respectively. Sodium chloride (<or=7.5 mM) was found to have no effect on biopolymer interactions, but interfered with interactions at higher levels (>7.5 mM) due to substantial PPI aggregation. The pH at which maximum PPI-GA interactions occurred was 3.5 and was independent of NaCl levels. As PPI-GA ratios increased, structure-forming transitions shifted to higher pH.


Food Chemistry | 2013

Microcapsule production employing chickpea or lentil protein isolates and maltodextrin: Physicochemical properties and oxidative protection of encapsulated flaxseed oil

Asli Can Karaca; Michael T. Nickerson; Nicholas H. Low

Flaxseed oil was microencapsulated, employing a wall material matrix of either chickpea (CPI) or lentil protein isolate (LPI) and maltodextrin, followed by freeze-drying. Effects of oil concentration (5.3-21.0%), protein source (CPI vs. LPI) and maltodextrin type (DE 9 and 18) and concentration (25.0-40.7%), on both the physicochemical characteristics and microstructure of the microcapsules, were investigated. It was found that an increase in emulsion oil concentration resulted in a concomitant increase in oil droplet diameter and microcapsule surface oil content, and a decrease in oil encapsulation efficiency. Optimum flaxseed oil encapsulation efficiency (∼83.5%), minimum surface oil content (∼2.8%) and acceptable mean droplet diameter (3.0 μm) were afforded with 35.5% maltodextrin-DE 9 and 10.5% oil. Microcapsules, formed by employing these experimental conditions, showed a protective effect against oxidation versus free oil over a storage period of 25 d at room temperature.


Journal of Agricultural and Food Chemistry | 2010

Intermolecular Interactions during Complex Coacervation of Pea Protein Isolate and Gum Arabic

Shuanghui Liu; Yuan-Long Cao; Supratim Ghosh; Dérick Rousseau; Nicholas H. Low; Michael T. Nickerson

The nature of intermolecular interactions during complexation between pea protein isolate (PPI) and gum arabic (GA) was investigated as a function of pH (4.30-2.40) by turbidimetric analysis and confocal scanning microscopy in the presence of destabilizing agents (100 mM NaCl or 100 mM urea) and at different temperatures (6-60 degrees C). Complex formation followed two pH-dependent structure-forming events associated with the formation of soluble and insoluble complexes and involved interactions between GA and PPI aggregates. Complex formation was driven by electrostatic attractive forces between complementary charged biopolymers, with secondary stabilization by hydrogen bonding. Hydrophobic interactions were found to enhance complex stability at lower pH (pH 3.10), but not with its formation.


Food Chemistry | 2012

Chitosan-tripolyphosphate submicron particles as the carrier of entrapped rutin.

K. Konecsni; Nicholas H. Low; Michael T. Nickerson

Chitosan (CH)-tripolyphosphate (TPP) submicron particles were formed as carriers of entrapped rutin, and the release properties characterized using simulated gastric juices and fluids of the small intestine. Particle size, charge and entrapment efficiencies were investigated as a function of the CH:TPP molar ratio (2.0:1.0-5.0:1.0). Size was found to decrease from ~814 nm for the 2.0:1:0 mass ratio to ~528 nm for the ratios between 2.5:1.0 and 4.0:1.0, and then again to ~322 nm for the 5:0:1.0 mass ratio, whereas all particles carried a positive surface charge, increasing from +21 to +59 mV as the ratio increased from 2.0:1.0 to 5.0:1.0. The percent entrapment was found to rise from 3.68% to 57.6% as the ratios increased from 2.0:1:0 to 4.0:1:0, before reaching a plateau. Submicron particles (4.0:1.0 mass ratio only) were found to retain rutin in simulated gastric fluids, whereas in conditions which simulated fluids from the small intestine, only 20% of the entrapped rutin was released and 80% remained absorbed to the CH:TPP carriers. Such particles have applications for the delivery of phenolics in food and natural health products.


Food Chemistry | 2015

Incorporation of phenolic compounds, rutin and epicatechin, into soy protein isolate films: mechanical, barrier and cross-linking properties.

Kara Friesen; Chang Chang; Michael T. Nickerson

Edible films prepared from soy protein isolate (SPI), with and without the phenolic compounds, rutin and epicatechin, as cross linking agents, were tested for their mechanical, optical and water vapour barrier properties. The addition of rutin significantly increased puncture strength (9.3N) over SPI alone (6.4N) whereas epicatechin had no effect. Tensile strengths of SPI films with rutin and epicatechin were similar (35.1 MPa and 22.1 MPa, respectively) and significantly stronger than films without added phenolics (9.3 MPa). SPI films without phenolics showed the greatest flexibility, as measured by tensile elongation. The addition of epicatechin was found to increase water vapour permeability significantly to 2.3 g mm/m(2)h kPa from 1.7 g mm/m(2)h kPa for SPI alone whereas rutin decreased water vapour permeability to 1.2 g mm/m(2)h kPa. Films without phenolics had lower opacity values than had those with phenolics. Findings indicate that rutin and epicatechin may be used as a natural means for improving specific properties of SPI films.


Frontiers in Microbiology | 2015

Probiotic-based strategies for therapeutic and prophylactic use against multiple gastrointestinal diseases.

Michael T. Nickerson; Darren R. Korber

Probiotic bacteria offer a number of potential health benefits when administered in sufficient amounts that in part include reducing the number of harmful organisms in the intestine, producing antimicrobial substances and stimulating the body’s immune response. However, precisely elucidating the probiotic effect of a specific bacterium has been challenging due to the complexity of the gut’s microbial ecosystem and a lack of definitive means for its characterization. This review provides an overview of widely used and recently described probiotics, their impact on the human’s gut microflora as a preventative treatment of disease, human/animal models being used to help show efficacy, and discusses the potential use of probiotics in gastrointestinal diseases associated with antibiotic administration.


Journal of Agricultural and Food Chemistry | 2013

Encapsulation of flaxseed oil using a benchtop spray dryer for legume protein-maltodextrin microcapsule preparation.

Can Karaca A; Nicholas H. Low; Michael T. Nickerson

Flaxseed oil was microencapsulated employing a wall material matrix of either chickpea (CPI) or lentil protein isolate (LPI) and maltodextrin using a benchtop spray dryer. Effects of emulsion formulation (oil, protein and maltodextrin levels) and protein source (CPI vs LPI) on the physicochemical characteristics, oxidative stability, and release properties of the resulting capsules were investigated. Microcapsule formulations containing higher oil levels (20% oil, 20% protein, 60% maltodextrin) were found to have higher surface oil and lower encapsulation efficiencies. Overall, LPI-maltodextrin capsules gave higher flaxseed oil encapsulation efficiencies (∼88.0%) relative to CPI-maltodextrin matrices (∼86.3%). However, both designs were found to provide encapsulated flaxseed oil protection against oxidation over a 25 d room temperature storage study relative to free oil. Overall, ∼37.6% of encapsulated flaxseed oil was released after 2 h under simulated gastric fluid, followed by the release of an additional ∼46.6% over a 3 h period under simulated intestinal fluid conditions.


Food Chemistry | 2016

Microencapsulation of canola oil by lentil protein isolate-based wall materials

Chang Chang; N. Varankovich; Michael T. Nickerson

The overall goal was to encapsulate canola oil using a mixture of lentil protein isolate and maltodextrin with/without lecithin and/or sodium alginate by spray drying. Initially, emulsion and microcapsule properties as a function of oil (20%-30%), protein (2%-8%) and maltodextrin concentration (9.5%-18%) were characterized by emulsion stability, droplet size, viscosity, surface oil and entrapment efficiency. Microcapsules with 20% oil, 2% protein and 18% maltodextrin were shown to have the highest entrapment efficiency, and selected for further re-design using different preparation conditions and wall ingredients (lentil protein isolate, maltodextrin, lecithin and/or sodium alginate). The combination of the lentil protein, maltodextrin and sodium alginate represented the best wall material to produce microcapsules with the highest entrapment efficiency (∼88%). The lentil protein-maltodextrin-alginate microcapsules showed better oxidative stability and had a stronger wall structure than the lentil protein-maltodextrin microcapsules.


Journal of Agricultural and Food Chemistry | 2011

Lentil and chickpea protein-stabilized emulsions: optimization of emulsion formulation.

Asli Can Karaca; Michael T. Nickerson; Nicholas H. Low

Chickpea and lentil protein-stabilized emulsions were optimized with regard to pH (3.0-8.0), protein concentration (1.1-4.1% w/w), and oil content (20-40%) for their ability to form and stabilize oil-in-water emulsions using response surface methodology. Specifically, creaming stability, droplet size, and droplet charge were assessed. Optimum conditions for minimal creaming (no serum separation after 24 h), small droplet size (<2 μm), and high net droplet charge (absolute value of ZP > 40 mV) were identified as 4.1% protein, 40% oil, and pH 3.0 or 8.0, regardless of the plant protein used for emulsion preparation.

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Andrea K. Stone

University of Saskatchewan

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Nicholas H. Low

University of Saskatchewan

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Chang Chang

University of Saskatchewan

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Darren R. Korber

University of Saskatchewan

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Ricky S.H. Lam

University of Saskatchewan

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Pierre Hucl

University of Saskatchewan

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Robert T. Tyler

University of Saskatchewan

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Asli Can Karaca

University of Saskatchewan

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