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Natallia Varankovich,Maria F. Martinez,Michael T. Nickerson,Darren R. Korber 한국식품과학회 2017 Food Science and Biotechnology Vol.26 No.1
Pea protein-alginate microcapsules with or without a chitosan coating and containing Lactobacillus rhamnosus R0011 and L. helveticus R0052 were produced by extrusion and tested for survivability during storage and in an in vitro gastrointestinal environment. Both microcapsule formulations provided significant protection for cells incubated in synthetic stomach juice at 37oC for 2 h, followed by 3 h in simulated intestinal fluid, relative to non-encapsulated bacteria. However, evaluation of cell viability during 9 weeks of storage at room temperature revealed that chitosan coating significantly improved microcapsule performance compared to non-coated microcapsules. Refrigerated storage had no negative impact on the microcapsule protection ability of both types of microcapsules. Notably, chitosan-containing microcapsules showed much higher bacterial survival counts during challenge tests even after storage. Moreover, the addition of chitosan to the microcapsule formulation did not increase the microcapsule size.
Andrea K. Stone,Anzhelika Teymurova,Chang Chang,Lamlam Cheung,Michael T. Nickerson 한국식품과학회 2015 Food Science and Biotechnology Vol.24 No.4
Electrostatic interactions within mixtures of a canola protein isolate (CPI) and both low (LMP) and highmethoxyl (HMP) pectin were investigated as a function of mixing ratio (1:1 to 30:1; CPI-pectin) and pH (8.0-1.5) using turbidity and electrophoretic mobility measurements during an acid titration. The rheological (flow behavior) and functional (solubility, foaming, and emulsifying properties) attributes of CPI-pectin complexes were also studied. Increasing biopolymer mixing ratios shifted critical pH values associated with formation of soluble and insoluble complexes to higher values until plateauing at approximately 10:1. Maximum coacervation of CPI-HMP and CPI-LMP mixtures occurred at pH values of 5.3 and 4.8, respectively, and at a 10:1 mixing ratio. The functionality of formed complexes was similar to CPI alone, except for a slight increase in solubility for the CPI-HMP system and a reduction in foaming capacity for CPI-LMP mixtures. For both mixed systems, viscosity was enhanced relative to CPI alone, showing greater pseudoplastic behavior.
Functional Properties of Protein Isolates from Different Pea Cultivars
Andrea K. Stone,Nicole A. Avarmenko,Tom D. Warkentin,Michael T. Nickerson 한국식품과학회 2015 Food Science and Biotechnology Vol.24 No.3
Surface characteristics and functional attributes of protein isolates prepared from different pea cultivars using isoelectric precipitation were investigated. Protein levels of isolates ranged from 81-89% with isoelectric points occurring between pH 4.7-4.9. Surface hydrophobicity values differed among cultivars with CDC Dundurn and CDC Striker isolates having the lowest and highest values, respectively. Protein solubility values at pH 7.0 varied with MFR042 and CDC Dundurn isolates displaying the lowest (approximately 54%) and highest (approximately 76%) values, respectively. No significant (p>0.05) differences existed between cultivar isolates for water hydration and oil holding capacity values. Cooper and CDC Dundurn isolates had significantly (p<0.05) lower emulsifying activity indices (EAI) (approximately 31-33 m2/g) than the other cultivars. Emulsifying stability index values were all similar. EAI values were positively correlated with surface hydrophobicity values and negatively correlated with solubility values. Varietal differences for the functional attributes of solubility and emulsification were identified.
Jiapei Wang,Darren R. Korber,Nicholas H. Low,Michael T. Nickerson 한국식품과학회 2015 Food Science and Biotechnology Vol.24 No.2
Highly acid-sensitive Bifidobacterium adolescentis (ATCC 15703) cells were entrapped in pea, soy, faba, and lentil protein-alginate capsules and subjected to challenge studies in synthetic gastric juice (SGJ, pH 2.5/37oC) and intestinal fluids (SIF, pH 6.5/37oC). B. adolescentis cells trapped in pea, soy, faba, and lentil protein-alginate capsules showed 1.9, 3.3, 5.1, and 5.5 log reductions in cell numbers, respectively after a 2 h challenge. Release of encapsulated B. adolescentis cells in SIF over 3 h indicated that after the first 10 min, almost all cells were released, regardless of the wall material. Storage of pea protein-based capsules was also tested in commercial orange, pineapple, and white grape juices at 4 and 22℃ for a 6-week duration. Encapsulated B. adolescentis cells survived in pineapple and white grape juice, but not in orange juice.
Ashish Singhal,Andrea K. Stone,Albert Vandenberg,Robert Tyler,Michael T. Nickerson 한국식품과학회 2016 Food Science and Biotechnology Vol.25 No.6
The functionality and surface characteristics of protein isolates prepared from seven genotypes of faba bean were investigated. All factors studied were independent of genotype. The average protein and isolate (~94% protein) yields were ~77% and ~25%, respectively, using an alkaline extraction process followed by isoelectric precipitation. The overall averages were: surface charge +22.1 mV, surface hydrophobicity 47.2 arbitrary units, and surface and interfacial tensions of 65.0 mN/ m and 10.7 mN/m, respectively. The ratio of the major globulin fractions (legumin:vicilin) shifted from 3.8 for the flours to 4.5 in the isolates. Average values for foaming capacity and stability, emulsion capacity, creaming stability, oil holding capacity, emulsifying activity and stability indices, and solubility were 162.0%, 65.0%, 184.0 g/g, 94.0%, 5.7 g/g, 13.0 m2/g, 10.7 min, and 81.0%, respectively. The lack of significant varietal effects would be advantageous to food processors as the source of the feedstock would not affect ingredient functionality.
Singhal, Ashish,Stone, Andrea K.,Vandenberg, Albert,Tyler, Robert,Nickerson, Michael T. 한국식품과학회 2016 Food Science and Biotechnology Vol.25 No.6
The functionality and surface characteristics of protein isolates prepared from seven genotypes of faba bean were investigated. All factors studied were independent of genotype. The average protein and isolate (~94% protein) yields were ~77% and ~25%, respectively, using an alkaline extraction process followed by isoelectric precipitation. The overall averages were: surface charge +22.1 mV, surface hydrophobicity 47.2 arbitrary units, and surface and interfacial tensions of 65.0 mN/m and 10.7 mN/m, respectively. The ratio of the major globulin fractions (legumin:vicilin) shifted from 3.8 for the flours to 4.5 in the isolates. Average values for foaming capacity and stability, emulsion capacity, creaming stability, oil holding capacity, emulsifying activity and stability indices, and solubility were 162.0%, 65.0%, 184.0 g/g, 94.0%, 5.7 g/g, $13.0m^2/g$, 10.7 min, and 81.0%, respectively. The lack of significant varietal effects would be advantageous to food processors as the source of the feedstock would not affect ingredient functionality.