PROTEINS AND PROTEIN FOODS

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PROTEIN Food & Ingredients FAQ		to Top REFERENCES to Top Aberle, E. D.; Merkel, R. A. 1966. Solubility And Electrophoretic Behavior Of Some Proteins Of Post-Mortem Aged Bovine Muscle. Journal of Food Science 31:151 Protein, Beef Postmortem, Beef Protein Solubility Adolph, W. H.; Shammas, E. I.; Halaby, S. H. 1955. The Nutritive Value Of Legume Proteins And Legume-Wheat Mixed Proteins In Near East Diets. Food Research 20:31 Legume, Protein, Near East Diet Adolph, W. H.; Wu, M. Y. 1934. The Influence Of Roughage On Protein Digestibility. Journal of Nutrition 7:381 Roughage, Protein Digestibility Aguilera, J.M. 1989. Protein extraction from lupin seeds: microstructural aspects and hypotehsis of mechanism. International Journal of Food Science and Technology 24: 29-37. Summary Protein was extracted into water 9pH8.0, 1 h) from defatted lupin seed kernel particles (mean theta, 1425 micrometer). Intact and extracted particles were examined by scanning and transmission electron microscopy. The innter surface of the cell wall initially showed several small holes considered as possible sites of plasmodesmata. During extraction, protein bodies first became disrupted into smaller microstrucctures and then protein dissolved. Wide passages were formed between cells which allowed transport of protein. The molecular weight of proteins in solution did not change with time, suggesting that bulk flow rather than selective transport predominated. Aguilera, J.M. and H.D. Garcia. 1989. Protein extraction from lupin seeds: a mathematical model. International Journal of Food Science and Technology 24: 17-27. Summary The effect of particle size and microstructural modification on protein extraction from defatted lupin was studied. Particles of different sizes (128-1425 micrometer) from untreated (control), flaked and exploded samples were extracted at pH 8.0-8.5 and different temepratures. A three-parameter kinetic model as well as a diffusional model were fitted to data. The yield of protein from the surface of particles, and the total extracted protein yield increased as particle size decreased, while the first order rate constant increased slightly or remained constant. Diffusion coefficients varied between 0.5 and 4.5x10 to the twelth m squared s minus one and were higher in exploded and flaked material than in the control. The energy of activation for diffusion was 43 kJ mol minus one. Differences in microstructure were stduied by scanning electron microscopy. Akeson, W. R.; Stahmann, M. A. 1965. Leaf Proteins As Foodstuffs, Nutritive Value Of Leaf Protein Concentrate, And In Vitro Digestion Study. Journal Of Agricultural And Food Chemistry 13:145 Leaf Protein Concentrate Albanese, A. A. 1947. The Amino Acid Requirements Of Man. Advances In Protein Chemistry 3:227 Amino Acid Requirement, Review Article Alexander, O. R.; Sallee, E. D.; Taylor, L. V. 1943. Variations In Chemical Composition Of Raw And Canned Peas. Food Research 8:254 Pea Solid, Canned Pea, Pea Moisture, Pea Ash, Pea Fat, Pea Protein, Pea Crude Fiber, Pea Carbohydrate, Pea Calcium, Pea Magnesium, Pea Calorie Allison, J. B.1953. Dietary Proteins. Their Function In Health And Disease. Journal Of Agricultural And Food Chemistry 1:71 Body Nitrogen, Dietary Protein, Tissue, Catabolism, Nitrogen Balance, Methionine, Vitamin Retention

Review Article, Biological Value, Nitrogen Retention, Production Ratio, Protein Efficiency Ratio, Nitrogen Balance Index, Biological Efficiency

Almquist, H. J. 1956. Fish Meal Stability, Changes In Fat Extractability And Protein Digestibility In Fish Meal During Storage. Journal Of Agricultural And Food Chemistry 4:638

Protein Digestibility, Fish Meal, Storage

Almquist, H. J.; Stokstad, E. L. R.; Halbrook, E. R. 1935. Supplementary Values Of Animal Protein Concentrates In Chick Rations. Journal of Nutrition 10:193

Animal Protein Concentrate, Chick Diet, Casein Nitrogen, Casein Protein, Casein Tryptophan, Casein Protein Quality Index, Sardine Meal Nitrogen, Sardine Meal Protein, Sardine Meal Tryptophan, Sardine Meal Protein Quality Index, Dogfish Meal Protein Quality Index, Tankage Protein Quality Index, Meat Scrap Protein Quality Index, Crackling Protein Quality Index, Menhaden Meal Protein Quality, Whale Meat Meal Protein Quality Index, Gelatin Protein Quality Index, Gelatin Tryptophan, Whale Meat Tryptophan, Tryptophan, Crackling Tryptophan, Meat Scrap Tryptophan, Tankage Tryptophan

Altschul, A. M. 1969. Food: Proteins For Humans. Chemical And Engineering News 47(49):68

Protein

Ambe, K. S.; Tappel, A. L. 1961. Oxidative Damage To Amino Acids, Peptides And Proteins By Radiation. Journal of Food Science 26:448

Irradiated Amino Acid, Irradiated Protein, Irradiated Peptide

Anderson, M. L.; Ravesi, E. M. 1970. On The Nature Of Altered Protein In Cod Muscle Stored At -29c After Aging In Ice. Journal of Food Science 35:199

Phase Contrast Microscope, Cod, Myotome Tissue, Cod, Protein, Cod, Sedimentation

Anderson, M. L.; Ravesi, E. M. 1970. On The Nature Of The Association Of Protein In Frozen-Stored Cod Muscle. Journal of Food Science 35:551

Frozen Cod, Cod Protein

Anderson, M. L.; Steinberg, M. A. 1964. Effect Of Lipid Content On Protein-Sodium Linolenate Interaction In Fish Muscle Homogenates. Journal of Food Science 29:327

Fish Lipid

Anfinsen, C. B.; Redfield, R. R. 1956. Protein Structure In Relation To Function And Biosynthesis. Advances In Protein Chemistry 11:1

Ovalbumin, Review Article, Lysozyme, Collagen, Papain, Protein Biosynthesis

Anson, M. L. 1945. Protein Denaturation And The Properties Of Proteins Groups. Advances In Protein Chemistry 2:365

Protein Denaturation, Protein

Armstrong, R. H. 1951. Amino-Acids In The Proteins Of Herbage. Journal Of The Science Of Food And Agriculture 2:166

Herbage, Amino Acid

Ashworth, A.; Harrower, A. D. B. 1967. Protein Requirements In Tropical Countries: Nitrogen Losses In Sweat And Their Relation To Nitrogen Balance. British Journal of Nutrition 21:833

Nitrogen Loss, Nitrogen Balance, Sweat, Protein Requirement

Aylward, F.; Haisman, D. R. 1969. Oxidation Systems In Fruits And Vegetables - Their Relation To The Quality Of Preserved Products. Advances In Food Research 17:1

Oxidizing Enzyme, Protein Efficiency Ratio, Oxidase, Catalase, Cytochrome Oxidase, Diphenol Oxidase, Ascorbate Oxidase, Amine Oxidase, Glycolate Oxidase, Respiratory Enzyme, Fermentatory Enzyme, Pectic Enzyme, Chlorophyllase, Lipoxygenase, Vegetable, Enzyme, Review Article

Aziz, J.; Tan, T. N.; Sediautama, A. D. 1968. The Protein Efficiency Ratio (Per) Of Fish Flour From Fish Preparation As Commonly Consumed In Indonesia. Paediatics Of Indonesia 8:1

Protein Efficiency Ratio, Fish Flour, Fish, Indonesia

Bai, Y., T.R. Sosnick, L. Mayne, S.W. Englander. 1995July 14. Protein folding intermediates: native-state hydrogen exchange. Science 269: 192.

Abstract The hydrogen exchange behavior of native cytochrome c in low concentrations of denaturant reveals a sequence of metastable, partially unfolded forms that occupy free energy levels reaching up to the fully unfolded state. The step from one form to another is accomplished by the unfolding of one or more cooperative units of structure. The cooperative units are entire omega loops or mutually stabilizing pairs of whole helices and loops. The partially unfolded forms detected by hydrogen exchange appear to represent the major intermediates in the reversible, dynamic unfolding reactions that occur even at native conditions and thus may define the major pathway for cytochrome c folding.

Bailey, K. 1944. The Proteins Of Skeletal Muscle. Advances In Protein Chemistry 1:289

Review Article, Skeletal Muscle, Protein

Bailey, L. H.; Leclere, J. A. 1935. Cake And Cake Making Ingredients. Cereal Chemistry 12:175

Cakemaking, Cake, Cake Formula, Gold Cake, Sponge Cake, Silver Cake, Chocolate Cake, Devil's Cake, Bread, Baked Product, Whole Wheat Bread, Soda Cracker, Cracker, Cookie, Doughnut, Macaroni, Noodle, Gingerbread, Gold Cake, Egg, Milk, Zwieback, Pilot Bread, Pretzel, Pretzel, Apple Pie, Squash Pie, Pie Crust, Matzoths, Saltine, Vanilla Wafers, Macaroon, Ginger Snap, Hot Cross Bun, Flour, Ash, Straight Grade Flour, Ash, Flour Ash, Flour Protein, Clear Flour, Angel Cake, Pound Cake

Baker, G. L. 1969. Nutritional Survey Of Northern Eskimo Infants And Children. American Journal Of Clinical Nutrition 22(5):612

Alaskan Nutritional Status, Eskimo Nutritional Status, Serum, Protein, Cholesterol, Infant, Children, Beckman Analytrol

Balasubramamian, S. C.; Ramachandran, M. 1958. Optimum Conditions Of Hydrolysis For Microbiological Assay Of Cystine In Food Proteins. Food Research 23:119

Cystine, Hydrolysis, Microbial

Baldwin, R. R.; Lowry, J. R.; Thiessen, R. Jr. 1951. Some Effects Of Processing On The Nutritive Properties Of Proteins. Food Research 16:107

Protein Processing

Balls, A. K.; Swenson, T. L. 1936. Dried Egg-White. Food Research 1:319

Dried Egg White Trypsin, Dried Egg White Reducing Sugar, Dried Egg White Pigment, Dried Egg White Nutrient Composition, Dried Egg White Protein, Dried Egg White Carbohydrate, Meringue, Cake Texture, Cake Beating Time

Barham, H. N. Jr.; Johnson, J. A. 1951. The Influence Of Various Sugars On Dough And Bread Properties. Cereal Chemistry 28:463

Sucrose, Glucose, Fructose, Invert Sugar, Flour Protein, Flour Ash, Flour Absorption, Amylograph, Dough Mixing, Sponge Dough, Mixing, Sensory Evaluation, Bread Grain, Bread Texture, Bread Crumb Firmness, Dough, Gas Production

Batcher, O. M.; Gilpin, G. L.; Duckworth, N. R.; Finkel, P. W. 1964. Eating Quality Of Quick-Cured Ham. Journal of Home Economics 56:758

Quick-Cured Ham, Curing, Ham Fat, Ham Protein, Shear Value, Ham Flavor, Ham Tenderness, Ham Juiciness, Ham Drip Loss, Ham Cooking Loss, Ham Weight, Ham Cooking Time, Biceps Femoris, Semimembranosus, Adductor, Rectus Femoris, Kramer Shear Press, Sensory Evaluation

Bate-Smith, E. C.; Bendall, J. R. 1945. Heat Coagulation Of Muscle Proteins. Nature 156:632

Muscle Coagulation, Protein Coagulation

Beaty, A.; Conlan, F. J.; Mcminn, S.; Weisberg, S. M. 1957. Protein Assay, Assessing Protein Quality With The Individual Protein-Depleted Chick. Journal Of Agricultural And Food Chemistry 5:541

Protein Analysis, Chick, Poultry, Protein Depletion

Beauchene, R. E.; Mitchell, H. L. 1957. Dehydration Temperature, Effects, Effect Of Temperature Of Dehydration On Proteins Of Alfalfa. Journal Of Agricultural And Food Chemistry 5:762

Alfalfa, Protein, Dried Alfalfa, Dehydration

Bell, L., P.B. Acousta and L. Chan. 1982June. Amino acid content of low-protein recipes. Journal American Dietetic Journal 80:579.

Bender, A. E. 1966. Nutritional Effects Of Food Processing Journal Of Food Technology 1:261

Nutrient Retention, Vitamin, Protein, Processing, Heat

Bensabat, L.; Frampton, V. L.; Allen, L. E.; Hill, R. A. 1958. Heat Effects On Peanut Proteins, Effect Of Processing On The E-Amino Groups Of Lysine In Peanut Proteins. Journal Of Agricultural And Food Chemistry 6:778

Peanut Protein, Peanut Processing, Peanut Lysine, Peanut Amino Group

Benson, S.W., D.A. Ellis, and R.W. Zwanzig. 1950. Surface areas of proteins. III. Adsorption of water. Journal American Chemical Society 72: 2102.

Beveridge, T., S.J. Toma, and S. Nakai. 1974. Determination of SH- and SS- groups in some food proteins using Ellman's reagent. Journal Food Science 39: 49.

Biale, J. B. 1960. The Postharvest Biochemistry Of Tropical And Subtropical Fruits. Advances In Food Research 10:293

Tropical Fruit, Subtropical Fruit, Postharvest Physiology, Biological Oxidation, Review Article, Nonclimacteric Fruit, Lemon, Avocado, Climacteric Fruit, Banana, Cherimoya, Feijoa, Fig, Grape, Grapefruit, Mango, Orange, Passion Fruit, Sapote, Papaya, Papaw, Citric Acid, Malic Acid, Persimmon, Carbohydrate, Sugar, Fat, Protein, Acid, Ash, Calcium, Phosphorus, Iron, Thiamin, Riboflavin, Niacin, Ascorbic Acid, Glucose, Fructose, Sucrose, Brix, Reducing Sugar, Flavor, Ascorbic Acid, Ethylene-Forming Mechanism, Pectin Formation, Fatty Acid

Bigelow, C.C. 1967. On the average hydrophobicity of proteins and the relation between it and protein structure. Journal Theoretical Biology 16: 187.

Bing, F. C.; Adams, W. L.; Bowman, R. O. 1932. The Protein Requirements Of The Albino Mouse. Journal of Nutrition 5:571

Mouse, Protein Requirement

Biro, N. A.; Balint, M. 1966. Studies On Proteins And Protein Complexes Of Muscle By Means Of Proteolysis. I. Influence Of Ionic Milieu On The Proteolysis Of Myosin. Acta Biochimica Et Biophysica Academiae Scientiarum Hungaricae 1:13

Myosin, Muscle Proteolysis, Meromyosin, Muscle Protein, Diisopropylfluorophosphate, Trypsin

Bixler, E. G.; Combs, G. F.; Shaffner, C. S. 1969. Effect Of Protein Level On Carcass Composition Of Turkeys. Poultry Science 48:261

Turkey Carcass, Moisture, Fat, Turkey Protein

Black, A.; Kahlenberg, O. J.; Bratzler, J. W.; Forbes, E. B. 1937. The Utilization Of Energy Producing Nutriment And Protein As Affected By Deficiency Of Iron And Copper. Journal of Nutrition 14:521

Nutriment, Protein, Iron, Copper

Black, M. M.; Schwartz, H. M. 1950. South African Fish Products. Xxx. Seasonal Changes In The Composition Of The Pilchard (Sardina Ocellata Jenyns). Journal Of The Science Of Food And Agriculture 1:182

Pilchard, Pilchard Oil, Oil, Saponification, Pilchard Fat, Pilchard Water, Pilchard Protein, Pilchard P2o5, Pilchard Vitamin A, Pilchard Oil Yield

Block, R. J. 1945. Amino Acid Composition Of Food Proteins Advances In Protein Chemistry 2:119

Protein, Leafy Vegetable, Arginine, Histidine, Lysine, Tyrosine, Tryptophan, Phenylalanine, Cystine, Methionine, Threonine, Isoleucine, Valine, Glycine, Glutamic Acid, Rice, Corn Germ, Oat, Wheat Germ, Flour, Wheat, Corn, Gluten, Arachin, Cottonseed Globulin, Soybean Meal, Gliadin, Zein, Edestin, Cottonseed Meal, Peanut Meal, Linseed, Meal, Sesame Meal, Sunflower Seed, Brewers Yeast, Yeast

Blunt, K. 1916. Recent Work On Normal Adult Nutrition. Journal of Home Economics 8:623

Adult Nutrition, Fat, Sugar, Protein, Energy, Additive

Blunt, K.; Sumner, E. 1928. The Calcium Of Cheese. Journal of Home Economics 20:587

Cottage Cheese Calcium, Cottage Cheese Protein, Swiss Cheese Calcium, Swiss Cheese Protein, Cheddar Cheese Calcium, Cheddar Cheese Protein

Bryson, J.W., S.F. Betz, H.S. lu, D.J. Suich, H.X. Zhou, K.T. O'Neil, W.F. DeGrado. 1995. Protein design: A Hierarchic approach. Science 270: 935.

Carraway, K.L. and R.B. Triplett. 1970. Reaction of carbodimides with protein sulfhydryl groups. Biochim. Biophys. Acta 200: 564.

Chan, A.S.M., R.R. Pereira., H.M. Henderson, and G. Blank. 1992. A non-dairy frozen dessert utilizing pea protein isolate and hydrogenated canola oil. Food Technology 46(1): 88-92.

Concon, J.M. 1975. Rapid method for the determination of lysine in cereal grains without hydrolysis. Anal. Biochem. 66: 460.

Concon, J.M. 1975. Rapid method for the determination of lysine in cereal grains without hydrolysis. Anal. Biochem. 66: 460.

Conway-Jacobs, A. and M.L. Lewin. 1971. Isoelectric focusing in acrylamide gels. Use of amphoteric dyes as internal marketers for determination of isoelectric points. Anal. Biochem. 43: 394.

Cumper, C.W.N. 1953. The stabilization of foams by proteins. Trans. Faraday Soc. 49: 1360.

Damodaran, S. 1994. Structure-function relationship of food proteins. IN "Protein Functionality in Food Systems," ed. N.S. Hettiarachchy and G.R. Ziegler, pp. 1-38. Marcel Dekker, Inc., New York.

Dickinson, E. and G. Stainsby. 1987. Progress in the formulation of food emulsions and foams. Food Technology 41(9):74-81.

Ehrenstein, D. 1997August1. Feeling a protein's motion. Science 277:637.

Elizalde, B.E., D. Giaccaglia, A.M.R. Pilosof, and G.B. Bartholomai. 1991. Kinetics of liquid drainage from protein destabilized foams. Journal Food Science 56: 24-26, 30.

German, J.B., T.E. O'Neill and J.E. Kinsella. 1985. Film forming and foaming behavior of food proteins. Journal Am. Oil Chem. Sco. 62: 1358.

Graham, D.E. and M.C. Phillips. 1979. Proteins at liquid interfaces. I. Kinetics of adsorption and surface denaturation. Journal Colloid Interface Science 70(3): 403-414.

Graham, D.E. and M.C. Phillips. 1979. Proteins at liquid interfaces. III. Molecular structure of adsorbed films. Journal Colloid Interface Sci. 70(3):427-439.

Groninger, H.S. Jr. 1973. Preparation and properties of succinylated fish myofibrillar protein. Journal Agric. Food Chem. 21: 978.

Habeeb, A.F.S.A. 1968. Quantitation of conformational changes on chemical modification of proteins:L use of succinylated proteins as a model. Arch. Biochem. Biophys. 121: 652.

Halling, P.J. 1981. Protein-stabilized foams and emulsions. CRC Food Sci. 155: 155-203.

Hamann, D.D. 1987. Methods for measurement of rheological changes during thermally induced gelation of proteins. Food Technology 41(3):100.

Henley, E.C. and J.M. Kuster. 1994. Protein quality evaluation by protein digestibility-corrected amino acid scoring. Food Technology 48(4): 74-77.

Hoare, D.G. and D.E. Koshland. 1967. A method for the quantitative modification and estimation of carboxylic acid groups in proteins. Journal Biol. Chem. 242: 2447.

Holden, C. 1971. Fish flour: protein supplement has yet to fulfill expectations. Science 173: 410-412.

Holzman, David. 1994. Protein folding. American Scientist 82:267.

Holzman, David. 1996. Protein Folding. American Scientist 82:267.

Huang, Y.T. and J.E. Kinsella. 1987(6). Effects of phosphorylation on emulsifying and foaming properties and digestibility of yeast protein. Journal Food Science 52: 1684.

Johnson, T. and M. Zabik. 1981. Egg albumen proteins interactions in an angel food cake system. Journal Food Science 46: 1231.

Jones, B.L. and G.L. Lookhart. 1985(2). High performance liquid chromatographic separation of peptides for sequenching studies. Cereal Science 62(2):89-96.

Kato, A., K. Komatsu, K. Fujimoto, and K. Kobayashi. 1985. Relationship between surface functional properties and flexibility of proteins detected by the protease susceptibility. Journal Agricultural Food Chemistry 33: 931-934.

The relationships between the surface properties and the flexiblity of proteins were investigated. An attempt to detect the flexibility of protein structure was made by the protease digestion method. Ovalbumin and lysozyme were not susceptible to protease, suggesting rigid or folded molecules, while kappa-casein, beta-lactoglobulin, and bovine serum albumin were susceptible to protease, suggesting flexible molecules. The digestion velocity of proteins by alpha-chymotrypsin and trypsin was closely correlated. Good correlations were observed between the foaming powder and emulsifying activity and the digestion velocity of proteins. These results suggest that the flexibility of protein structure detected by protease digestion may be an important structural factor governing the foam formation and emulsification.

Kato, A. and S. Nakai. 1980. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta 624: 13.

Kim, S.H. and J.E. Kinsella. 1987. Surface active properties of food proteins: Effects of reduction of disulfide bonds on film properties and foam stability of glycinin. Journal Food Science 52(1):128.

Kim, S.H. and J.E. Kinsella. 1985. Surface activity of food proteins: relationships between surface pressure development, viscoelasticity of interfacial films and foam stability of govine serum albumin. Journal of Food Science 50: 1526.

Kinsella, J.E. 1976. Functional properties of proteins in foods: a survey. Crit. Rev. Food Sci. Nutr. 7(3):219-280.

Kinsella, J.E. 1981. Functional properties of proteins: possible relationships between structure and functions in foams. Food Chemistry 7(4): 273-288.

Kinsella, J.E. 1984. Milk proteins: physicochemical and functional properties. Crit. Rev. Food Sci. Nutr. 21(3): 197-262.

Kinsella, J.E. and K.J. Shetty. 1979. Chemical modification ofr improving functional properties of plant and yeast proteins. ACS Symposium Series 92: 37.

Kinsella, J.E. 1981. Functional properties of proteins: Possible relationships between structure and function in foams. Food chemistry 7: 273.

Kitabatake, N. and E. Doi. 1982. Surface tension and foaming of protein solutions. Journal Food Science 47: 1281-122, 1225.

Knightly, W.H. 1968. The role of ingredients in the formulation of whipped toppings. Food Technology 22: 731-744.

Knightly, W.H. 1969. The role of ingredients in the formulation of coffee whiteners. Food technology 23: 171-182.

Laemmli, U.K. 1970,August 15. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680.

Abstract Using an improved method of gel electrophoresis, many hithertho unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four major components of the head are cleaved during the process of assembly, apparently after the precursor proteins have assembled into some large intermediate structure.

Lawrence, R., F. Consolacion and P. Jelen. 1986March. Formation of structured protein foods by freeze texturization. Food Technology 40(3):77.

Lee, S.Y., C.V. Morr, and E.Y.W. Ha. 1990. Structural and functional properties of caseinate and whey protein isolate as affected by temperature and pH. Journal Food Science 57: 1210-1213, 1229.

Li-Chan, E., S. Nakai, and D.F. Wood. 1984. Hydrophobicity and solubility of meat proteins and their relationship to emulsifying properties. Journal Food Science 49: 345-350.

Linderstrom-Lang, K.U. 1953. How is a protein made? Scientific American (September)

MacRitchie, F. 1978. Proteins at interfaces. Adv. Protein Chem. 32: 283.

McGee, Harold. 1984. On Food and Cooking.The Science and Lore of the Kitchen. Collier Books. New York.

McLaren, A.D. and J.W. Rowen. 1951. Sorption of water vapor by proteins and polymers: a review. Journal Polymer Science 4: 289.

Mills, J. 1988November. Proteins with enzyme inhibitor activity. American Biotechnology Laboratory 6(8): 29-32.

Mullen, J.D. and D.E. Smith. 1968. Protein composition and solubility. Cereal Science Today 13: 398.

Murphy, K.P., P.L. Privalov, S.J. Gill. 1990February 2. Common features of protein unfolding and dissolution of hydrophobic compounds. Science 247:559.

Nakai, S. and E. Li-Chan. 1993. Recent advances in structure and function of food proteins: QSAR approach. Critical Reviews in Food Science and Nutrition 33(6): 477-499.

Abstract QSAR (quantitative structure-activity relationship), widely used in chemistry with hydrophobic electronic, and steric parameters as structural factors, was found to be appropriate for use with food proteins. despite the difficulty, due to the complexity in macromolecular structure, in defining the steric terms. Emulsifying ability was closely related to hydrophobicity, and incorporation of solubility to hydrophobicity as factors improved the Rsquared of regression analysis. Foaming activity required both hydrophobicity and other factors pertaining to the adsorption of proteins at the interface in order to obtain adequate foam lamella strength. Hydrophobicity as well as other factors relating to the intermolecular interactions, for example. Ca and SH are involved in thermally induced gelation. For breadmaking, although no extensive QSAR work had been carried out, the important function of high molecular glutenin subunits was confirmed, and notably, the critical function of hydrophobicity in breadmaking also was demonstrated. PLS (partial least-squares regression) and neural networks classify more correctly than other multivariate techniques, thereby yielding higher r squared values in modeling and predition. However, multiple regression analysis and PCR (principal component regression) also were found to be effective for modeling because the information useful in elucidating the mechanism of protein function could be readily obtained. A characteristic property of unsupervised learning techniques, especially PCS(principal component similarity analysis), in identifying influenctial factors in the function mechanisms was demonstrated.

Nakai, S. and E. Li-Chan. 1993. Recent advances in structure and function of food proteins: ASAR approach. Critical Reviews in Food Science and Nutrition 33(6):477-499.

Nakamura, T., S. Utsumi, and T. Mori. 1985. Effects of temperature on the different stages in thermal gelling of glycinin. Journal Agricultural Food Chemistry 33: 1201-1203.

Pauling, L., R.B. Corey, and R. Hayward. 1954July. The structure of protein molecules. Scientific American

Pawson, T. and J.D. Scott. 1997December. Signaling through scaffold, anchoring, and adaptor proteins. Science 278: 2075.

Pennisi, E. 1996July 26. Teams tackle protein preduction. Science 273: 426-428.

Presta, L.G. and G.D. Rose. 1988June. Helix signals in proteins. Science 240: 1632-1641.

Phillips, L.G., Z. Haque, and J.E. Kinsella. 1987. A method for the measurement of foam formation and stability. Journal Food Science 52: 1074.

Poole, S.I., C.L. West, and J. Walters. 1984. Protein-protein interactions: Their importance in the foaming of heterogenous protein systems. Sci. Food agric. 35: 701.

Regan, L. and W.F. DeGrado. 1988. Characterization of a helical protein designed from first principles. Science 241: 976.

Abstract The question of how the primary amino acid sequence of a protein determines its three-dimensional strcutre is still unanswered. One approach to this problem involves the de novo design of model peptides and proteins that should adopt desired three-dimensional structures. A systematic approach was aimed at the design of a four-helix-bundle protein. The gene encoding the designed protein was synthesized and the protein was expressed in Escherichia coli and purified to homogeneity. The protein was shown to be monomieric, highly helical, and very stable to denaturation by guanidine hydrocholoride (GuHCl). Thus a globular protein has been designed that is capable of adopting a stable, folded structure in aqueous solution.

Richardson, J.S. and D.C. Richardson. 1988June. Amino acid preferences for specific locations at the ends of alpha helices. Science 240: 1648.

Righettii, P.G. and J.W. Drysdale. 1974. Isoelectric focusing in gels. Journal Chromatog. 98: 271.

Righetti, P.G. and A.B. Bosisio. 1981. Applications of isoelectric focusing to the analysis of plant and food proteins. Electrophoresis 2: 65-75.

Rose, G.D., A.R. Geselowitz, G.J. Lesser, R.H. Lee, M.H. Zehfus. 1985August 30. Hydrophobicity of amino acid residues in globular proteins. Science 229: 834.

Sarwar, G., D.A. Christensen, A.J. Finlayson, M. Friedman., L.R. Hackler, S.L. Mackenzie, P.L. Pellett, and R. Tkachuk. 1983. Inter- and Intra-laboratory variation in amino acid analysis of food proteins. Journal Food Science 48(2): 526-531.

Sauter, E. and J. Montoure. 1972. The relationship of lysozyme content of egg white to volume and stability of foams. Journal Food Science 37: 918.

Service, R.F. 1997July11. Amino acid alchemy transmutes sheets to coils. Science 277: 179. Shimada, K. and S. Matsushita. 1980. Relationship between thermocoagulation of proteins and amino acid compositions. Journal Agric. Food Chem. 28: 413.

Shimada, K. and S. Matsushita. 1981. Effects of salts and denaturants on thermocoagulation of proteins. J. Agric. Food Chem. 29: 15.

Uken Sukaeni Sanusi Soetrisno. Characterization of yellow pea (Pisum sativum L. Miranda) Proteins and the Proteinate Functional Properties. M.S. Thesis.

Stein, W.H. and S. Moore. 1961, February. The structure of proteins. Scientific American. W.H. Freeman and Company. #80

Thompson, L.U., A.V. Tenebaum, and H. Hui. 1986. Effect of lectins and the mixing of proteins on rate of protein digestibility. Journal of Food Science 51:150.

Tomoaia-Cotisel, M., A. Sen, and P.J. Quinn. 1983. Surface-active properties of 1,2-distearolygalactosylglycerols. Journal of Colloid and Intrface Science 94(2):390.

Townsend, A.-A. and S. Nakai. 1983. Relationships between hydrophobicity and foaming characteristics of food proteins. Journal Food Science 48: 588-594.

hydrophobocity mesured fluorometrically for food proteins and pure proteins using cis-parinaric acid as a hydrophobic probe had significant correlations to foaming capacity when the proteins in solution were unfolded by heating in boiling water in the presence of 1.5% dodecyl sulphate prior to fluorometric measurement. Hydrophobicity measured without unfolding, which had previously shown a significant correlation to emulsification, was not significantly correlated with foaming capacity. Two highly significant regression equations were generated: one included hydrophobicity and dispersibility were associated with optimum foaming capacity. There was a singificant negative relationship between foam stability and charge density. Hydrophobicty and viscosity were also important in foam stability.

Tsutsui, T., E. Li-Chan and S. Nakai. 1986. A simple fluorometric method for fat-binding capacity as an index of hydrophobicity of proteins. Journal Food Science 51(5): 1268-1272.

VALLE-RIESTRA, J. AND R.H. BARNES. 1969 OR 1970. Digestion Of Heat-Damaged Egg Albumen By The Rat. Journal Nutrition 100: 873-882.

Voutsinas, L.P., E. Cheung And S. Nakai. 1983. Relationships Of Hydrophobicity To Emulsifying Properties Of Heat Denatured Proteins. Journal Food Science 48(1): 26-32.

Waniska, R. and J.E. Kinsella. 1979. Foaming properties of proteins: evaluation of a column aeration apparatus using ovalbumin. Journal Food Science 44: 1398.

Wickner, W. 1980November 21. Assembly of proteins into membranes. Science 210: 861.

Zaniquelli, M.E.D. and F. Galembeck. 1985. Modification of foam drainage by electroosmotic effect. Langmuir 1: 647-651.

Updated: Thursday, September 6, 2007.

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