bluuebunny/crossref_metadata_2025_split huggingface dataset:
Gram Negative Bacteria Associated with Sloughing, a Softening of California Ripe Olives
Authors: VAUGHN REESE H. , KING DOUGLAS , NAGEL CHARLES W. , NG HENRY , LEVIN ROBERT E. , MACMILLAN JAMES D. , II GEORGE K. YORK 
Published: August 2006

SUMMARY—A softening of olives, called “sloughing,” has occurred during the processing of California “ripe” olives for many years. The spoilage is characterized by the softening and ultimate sloughing of at least part of the skin and tissue from the pit of the olive. Control of the spoilage was accomplished largely by reducing the washing period from the customary four to a maximum of three days. The gram‐negative bacteria associated with the spoilage include species allocated to five different genera. Aerobacter, Escherichia, Paracolobactrum, Aeromonas, and Achromobacter. The characteristics of these bacteria, their ability to cause softening of olives, and the kinds of pectolytic enzymes they produce are described.
Effect of Processing on Recovery of Polio Virus From Inoculated Foods
Authors: HEIDELBAUGH NORMAN D. , GIRON DAVID J. 
Published: August 2006

SUMMARY—The recovery of polio virus inoculated into a variety of foods was studied as a function of four food processing operations: freeze dehydration, “pasteurization” by exposure to Cobalt‐60 gamma irradiation, refrigerated storage at 4°C, and storage at 20°C. In general, a decrease in virus recovery was noted following each of the operations. Complete loss in recoverability was observed only in highly acid foods (below pH 2.9) stored at 20°C for 96 or 168 hr. Use of a DEAE Sephadex chromatographic column was found to have potential application for separation of virus foods.
Heat Gelling Properties of Myosin, Actin, Actomyosin and Myosin‐subunits in a Saline Model System
Authors: SAMEJIMA K. , HASHIMOTO Y. , YASUI T. , FUKAZAWA T. 
Published: August 2006

SUMMARY—Myosin and actin were isolated from rabbit skeletal muscle. The gelation of myosin, actin and actomyosin, as well as of heavy and light meromyosins derived from myosin by trypsin treatment, by heat was studied in various systems. The data indicate that the heat gelling properties of these protein solutions do not run parallel with those of saline model systems composed of these proteins and stroma. Actin does not exert any influence on the binding properties of the system, but when F‐actin and myosin A were both present the resulting binding properties were considerably improved. Since heavy and light meromyosins have little influence on binding properties, it may be concluded that an intact molecule of myosin is required for development of binding properties upon heating.
Meat Pigment Changes in Intact Beef Samples
Authors: ZIMMERMAN G. L. , SNYDER H. E. 
Published: August 2006

SUMMARY—Reflectance spectrophotometry was used to study pigment changes in beef samples that (1) had been oxygenated and wrapped with an oxygen‐impermeable film, (2) had been treated with ferricyanide and (3) had either treatment (1) or (2) plus malonic acid. Treatment (1) showed a metmyoglobin (MetMb) accumulation of 30% in 30 min, followed by reduction of MetMb. Malonic acid inhibited oxygen utilization and MetMb‐reducing activity (MRA). Treatment (2) showed MRA that was inhibited by the presence of oxygen or malonic acid. Malonic acid inhibited oxygen utilization rather than directly inhibiting MRA.
Nicotinamide and Nicotinic Acid in Color Preservation of Fresh Meat
Authors: KENDRICK JEAN L. , WATTS BETTY M. 
Published: August 2006

SUMMARY—Nicotinamide (NAm) protected the metmyoglobin (MetMb), reducing activity and oxygen consumption of ground beef or pork on refrigeration or freezer storage. Nicotinic acid (NA) increased MetMb in aerobically refrigerated ground meats, while NAm, particularly in combination with ascorbic acid, decreased it. In model systems and meats, hemochrome formation occurred with reduced myoglobin and either NA or NAm, but more readily with NA and at lower pH values. No hemochrome was formed in aerobically stored meats with NA or NAm, even with ascorbic acid present. Anaerobic conditions gave hemochromes, but only at the higher concentrations and lower pHs tried. The implication of these findings to color protection in fresh meats is discussed.
High Resolution Vapor Analysis for Fruit Variety and Fruit Product Comparisons
Authors: FLATH R. A. , FORREY R. R. , TERANISHI R. 
Published: August 2006

SUMMARY By using a system incorporating large‐bore open‐tubular gas chromatographic columns, high resolution vapor analyses of five fresh apple products were run. The improved peak separation attainable with such a system permits more detailed comparisons between different samples. This is a considerable aid in varietal studies and in following loss and change of volatiles during processing. The apple varieties examined appear to differ mostly in the relative proportions of individual components rather than in the presence or absence of certain constituents.
Sapid Components in Carrot
Authors: OTSUKA HITOSHI , TAKE TSUNEKO 
Published: August 2006

SUMMARY: The relationship between various substances present in carrot to its taste was studied. Nucleic acid derivatives found in hot water extracts of carrot were adenine, adenosine, inosine, hypoxanthine, 5′‐AMP, 5′‐UMP, UDP, but 5′‐IMP and 5′‐GMP were absent. The contents of these derivatives were extremely small. Silica gel chromatography showed the presence of small quantities of succinic acid, α‐ketoglutaric acid, lactic acid, pyroglutamic acid, citric acid and glycolic acid.Amino acids in hot water extracts of carrot were detected by two‐dimensional thinlayer chromatography and automatic amino acid analyzer. Identified were glutamic acid, valine, leucine, aspartic acid, lysine, and serine etc. Glutamic acid content was relatively large. Sucrose, maltose and glucose were detected in carrot and these carbohydrates were responsible for the sweetness of carrot. The taste of carrot was due mainly to the presence of glutamic acid and the buffer action of various amino acids.
Low Temperature Growth of Type E Clostridium botulinum Spores. 2. Effects of Solutes and Incubation Temperature
Authors: EMODI A. S. , LECHOWICH R. V. 
Published: August 2006

SUMMARY— The inhibition of outgrowth of spores of Clostridium botulinum Type E by the addition of different concentrations of various solutes to a trypticase‐peptone‐sucrose‐yeast extract medium (TPSY) was studied at different incubation temperatures. Solutes added to TPSY medium were sodium chloride (NaCl), sodium formate (NaCOOH), potassium chloride (KCI), sucrose and glucose. Incubation was at 30, 21.1, 15.6, 10 and 7.2°C, and growth was confirmed by mouse toxin assay. The effect of the solutes on the equilibrium relative humidities (ERHI of the various media was measured using the graphical interpolation method and expressed as water activity (aw). The possibility of an osmotic effect was also investigated. The molar (M) concentrations and osmotic pressures of the different solutes were calculated and related to the approximate inhibitory concentrations of 5.0% NaCl (aw 0.975), 6.0% KCI (aw 0.974), 5.5% NeCOOH (aw 0.9711, 38.5% sucrose (aw 0.976) and 22.5%. glucose (aw 0.970).The inhibitory salt concentrations were approximately 0.80 M and produced osmotic pressures of about 36.0 atmospheres. The approximate osmotic pressure of the inhibitory 1.12 and 1.24 M sucrose and glucose solutions were 25.08 and 27.97 atmospheres respectively.Growth response decreased as the incubation temperature decreased as measured by delayed outgrowth times and in decreased amount of cellular material produced by the Type E strains tested.
Dihydrochalcone Sweeteners–Sensory and Stability Evaluation
Authors: INGLETT G. E. , KRBECHEK L. , DOWLING B. , WAGNER R. 
Published: August 2006

SUMMARY— The sensory and stability properties of neohesperidin dihydrochalcone were evaluated. Combinations of neohesperidin dihydrochalcone with saccharin and cyclamate were tested for their effect on taste qualities in soft drink type products. A mixture in which neohesperidin dihydrochalcone contributed 25% of the total sweetness (saccharin 64% and cyclamate 11%) gave a taste sensation that was considered to be of good quality. Tests indicated that the presence of neohesperidin dihydrochalcone gave, for most tasters, an apparent increase in flavor. The ethoxy homolog, homoneohesperidin dihydrochalcone, gave the same effect as the neohesperidin dihydrochalcone.The stabilities of neohesperidin dihydrochalcone under a variety of conditions of manufacture, storage and use were studied. Research showed that the glycosidic compound was resistant to hydrolysis of the sugar moieties in solutions of various acids above pH 2 at normal temperatures.
SOME PERSONALITY TRAITS RELATED TO PERFORMANCE IN A REPEATED SENSORY TASK
Authors: HENDERSON D. , VAISEY M. 
Published: August 2006

SUMMARY–Judges selected on the basis of high scores in need for achievement performed better than low scorers in flavor difference detection tests repeated 7 times in a 4‐wk period. Each test consisted of triangular, paired and degree of difference discriminations in 6 comparisons of varying difficulty devised from cakes made with fresh, dried and irradiated eggs. During the last 5 tests, high achievers showed significantly superior odd sample selection. Throughout the test period high achievers showed somewhat better discrimination of moderately difficult comparisons and a higher incidence of total responses. Degree of flavor difference expressed showed dependence on personality scores for aggression, nurturance, autonomy, harmavoidance and impulsivity.
The Effects of Freezing on the Survival of Salmonella and E. coli in Pacific Oysters
Authors: DIGIROLAMO R. , LISTON J. , MATCHES J. 
Published: August 2006

SUMMARY: A mixed inoculum of Salmonella derby or S. typhimurium and Escherichia coli I was injected into the intestinal region of Pacific oysters (Crassostrea gigas) which were then frozen by four methods. Frozen oysters were stored at O°F, and survival of the inoculated bacteria was determined over a period of two weeks. In separate experiments, inoculated oysters were homogenized and then stored, unfrozen, at 32°F and −30°F (frozen). Routinely, bacterial counts and pH readings were taken of all samples during the course of experiments.Both species of Salmonella proved to be highly sensitive to freezing, regardless of the freezing method, and showed a survival of 1% or less after 48 hr. E. coli proved less sensitive, showing a wide and capricious variability of survival during the first week of storage, with survival ranging from 10 to 30%. Generally, however, most samples showed a decline comparable to that of salmonellae after two weeks’storage. Because of the fluctuation in E. coli counts after freezing, it is difficult to correlate the numbers of E. colt in frozen shellfish with the count in unfrozen shellfish. Therefore, it would be inappropriate to apply coliform standards for fresh oysters to the frozen product.In separate studies using inoculated oyster homogenates held at 32° and −30°F for 168 hr, a higher survival rate of E. coli and salmonellae was noted in samples held at −30°F. However, since results obtained were based solely on bacterial counts, it is not possible to say with certainty that these results indicate a protective effect by oyster homogenates against the adverse effects of freezing. Significantly, the results of these experiments did not agree with results obtained with whole oysters, thus indicating the inadvisability of attempting to apply results of homogenate studies to the whole oyster.
INFLUENCE OF AGING ON THE ELECTROPHORETIC AND STRUCTURAL CHARACTERISTICS OF TURKEY BREAST MUSCLE
Authors: JOHNSON PAMELA G. , BOWERS JANE A. 
Published: August 2006

ABSTRACTElectrophoretic patterns of myofibrillar proteins and the ultrastructure of turkey breast muscle aged 0–48 hr were studied. Electrophoretic patterns indicated that protein aggregates were present in aged but not in unaged (0‐hr) muscle. Tropomyosin was present in 0‐hr muscle but not in muscle aged 3 hr or longer. General structural deterioration was noted as muscle aged. H‐zones were absent and M‐lines sometimes were displaced in transmission electron micrographs of post‐rigor muscle. Z‐lines lost their pre‐rigor density while corresponding transverse elements in scanning electron micrographs flattened during aging. Spaces developed between fibrils indicating loss of lateral attachments and breaks at the Z‐line were noted. Although protein and ultrastructural changes were limited, they possibly account for postmortem decrease in shear values.
FUNCTIONAL PROPERTIES OF ENZYME‐MODIFIED ACYLATED FISH PROTEIN DERIVATIVES
Authors: MILLER RUTH , GRONINGER HERMAN S. 
Published: August 2006

ABSTRACTEnzymemodified acylated protein derivatives were prepared with succinic and acetic anhydrides from washed fish muscle and were evaluted for their functionality. The degree of acylation and of hydrolysis by bromelain was studied to determine how these variables affect functionality of the protein. The degree of acylation was determined by measuring available epsilon amino groups of lysine. Susceptibility to hydrolysis was determined by treating with bromelain at different ratios of bromelain to substrate. The functional properties studied were emulsifying activity, emulsifying capacity, gelation, water absorption, aeration, and foam stability. These functional properties increased until 43–59% of the free amino groups were acylated. Further acylation had no significant effect. Hydrolysis of the acylated protein slightly lowered the emulsifying, gelation, and water absorption properties, but increased the aeration capacity of both the acetylated and succinylated proteins and the foam stability of the latter. The succinylated proteins displayed functional properties similar to those of the acetylated proteins. Succinylated proteins, however, yielded functionality slightly but significantly superior to that of acetylated proteins. The performance of enzyme‐modified acylated fish protein derivatives in food systems is also discussed.
EFFECT OF TEMPERATURE AND pH ON PROTEIN‐PROTEIN INTERACTION IN ACTOMYOSIN SOLUTIONS
Authors: DENG J. , TOLEDO R. T. , LILLARD D. A. 
Published: August 2006

ABSTRACTThe extent of protein‐protein interactions in actomyosin solutions was measured as a change in light scattering absorbance of a solution undergoing change. The extent of the reaction registered as an increase in light scattering absorbance indicating an increase in the size of the macromolecules. In treatments where the extent of protein‐protein interaction was extensive, film formation and/or precipitation of the macromolecules occurred. At constant protein concentration the kinetics of the reaction was dependent upon temperature, pH and the type of actomyosin used. In general, the rate and maximum extent of change increased with increasing temperatures and decreasing pH. Below 40° C more change was generally observed in beef actomyosin solution compared to mackerel at the same temperature and pH. However, at higher temperatures, mackerel actomyosin often shows more change than beef under the same conditions. The shapes of the reaction curves were such that the slope of the steepest line that can be drawn from the origin to tangent the curve at the region where the change starts to taper off (the characteristic slope), was a good index of the rate of change and the maximum extent of interaction attained. Arrhenius‐type plots of the characteristic slopes showed three possible mechanisms of change predominating within certain temperature ranges, as indicated by well‐defined inflections in the curves, reflecting varying activation energies for the reactions. The three temperature zones are: below 40°C; between 40 and 60° C; and above 60° C. Below 40° C the rate and maximum extent of protein‐protein interaction is very strongly temperature dependent.
EFFECTS OF TYROSINC MODIFICATION ON STABILIZING ABILITY OF KAPPA‐CASEIN
Authors: Ll E. C. Y. , NAKAI S. 
Published: August 2006

ABSTRACTChemical modifications of tyrosine residues in κ‐casein were carried out to study their role in Ca‐αS1 ‐caseinate stabilization. In accord with Woychik and Wondolowski (1969), the stabilizing ability decreased on nitration with tetranitromethane. Electrophoretic patterns showed aggregation of the modified κ‐casein when 8% polyacrylamide gel was used at pH 8.6, whereas the casein migrated faster than the unmodified casein in 1.2% agarose gel suggesting increased negativity on casein malecules upon nitration. However, O‐acetylation with N‐acetylimidazole, after protecting SH and amino groups, did not cause any significant differences from the control κ‐casein in stabilizing ability or in electrophoretic patterns. Therefore, tyrosine residues are not essential for the stabilizing ability of κ‐casein.
WATER BINDING OF MACROMOLECULES DETERMINED BY PULSED NMR
Authors: LEUNG H. K. , STEINBERG M. P. , WEI L. S. , NELSON A. I. 
Published: August 2006

ABSTRACTPulsed NMR was applied to measure the spin‐lattice (T1) and the spin‐spin (T1) relaxation times of the water adsorbed on sodium alginate, pectin, corn starch, casein and cellulose. T1 was determined by means of repeated 90°‐90° pulse sequences and T2 by the spin‐echo method. T1 relaxation time curves for all the samples studied showed simple exponential, i.e., single phase, behavior. Plots of T1 as a function of moisture content showed minima at 0.15–0.258 water/g dry matter; plots of T1 vs water activity (Aw) yielded minima at Aw of 0.65. T2 relaxation time curves for corn starch containing more than 0.56g water/g DM exhibited two‐phase behavior, indicating the existence of two water fractions of different mobility. The amount of water in the bound fraction showed a remarkable consistency (0.194 ± 0.011g water/g DM) among six samples of high moisture content. T2 was found to increase with moisture content for all the macromolecules. Cellulose showed exceptionally long T2 values compared to the other materials at the same moisture content, whereas pectin and sodium alginate showed short T2 values. These results indicated that T2 value is a measure of strength of water binding. Break points were observed in the T2‐moisture curve. The moisture contents at these points corresponded to the bound water content determined by freezing and to the equilibrium moisture content at Aw of 0.9. T2 increased exponentially with Aw.
ESTIMATION OF CHLOROPHYLL AND CAROTENOID CONTENTS OF WHOLE TOMATO BY LIGHT ABSORBANCE TECHNIQUE
Authors: WATADA ALLEY E. , NORRIS KARL H. , WORTHINGTON JOHN T. , MASSIE DAVIS R. 
Published: August 2006

ABSTRACTThe relationship between optical measurements of whole tomato and pigment content was studied. The difference between the absorbances (A) at 710 and 780 nm [ΔA (710–780 nm)] correlated significantly (r = 0.98) with chlorophyll contents of 0.3–13.4 μg/g fresh weight (gfw). The ΔA (570–780 nm) correlated significantly (r = 0.97) with lycopene contents of 0.2–46.7 μg/gfw. The ΔA (550–580 nm) correlated significantly with the β‐carotene, content (r = 0.95). The reflectance measurements correlated with the chlorophyll and lycopene contents, but the coefficients were lower and the standard errors were larger than those observed with the absorbance measurements.
INDUSTRIAL PRODUCTION OF SOY‐ENRICHED TORTILLA FLOUR BY LIME COOKING OF WHOLE RAW CORN‐SOYBEAN MIXTURES
Authors: DEL VALLE F. R. , MONTEMAYOR E. , URGES H. BO 
Published: August 2006

ABSTRACTPrevious work has established that it is possible to enrich home‐prepared tortillas with soy proteins by lime cooking of whole raw corn‐soybean mixtures. Since tortillas are also extensively prepared in Mexico from limed corn flour, an investigation was carried out to determine if it were possible to enrich such flour by a similar procedure. The normal process for making tortilla flour was employed, except that In the lime cooking step, whole raw corn‐soybean mixtures containing 10% soybeans were used in place of pure corn. Protein quantity and quality of the enriched flour were found to be increased as follows: protein content, from 9.2 to 12.6%, an increase of 36%; protein efficiency ratio (PER) from 1.45 to 2.62 (casein PER = 3.40), an increase of 81%. Heat treatment of the enriched flour was found to be adequate by the urease method, and a trained panel could not significantly distinguish between tortillas prepared from either flour. Finally, rancidity was not detected organoleptically in a sample of flour stored at room temperature for 12 months. Considering present costs of corn and soybeans in Mexico, it was calculated that use of whole raw soybeans as an enriching agent for tortilla flour at a 10% level would raise the cost of the flour by 5%, while use of defatted soy flour for the same purpose, and at an equivalent protein level, would raise the cost of the flour by 40%.
AUTOMATED ANALYSIS OF SORBIC ACID IN FOOD PRODUCTS
Authors: ROY R. B. , SAHN M. , CONETTA A. 
Published: August 2006

ABSTRACTThe increasing use of sorbic acid and sorbates has created a need for a rapid, reliable and accurate analytical procedure for the routine analysis of these materials in food products. In this paper is described an automated version of the most popular calorimetric (thiobarbituric acid) method, originally proposed by Schmidt. The procedure uses a gas diffusion membrane in lieu of steam distillation for the separation of sorbic acid from the food samples. The separated acid is cleaved with potassium dichromate in acidic medium to yield an intermediate malon‐aldehyde, which in turn, when reacted with thiobarbituric acid, produces a red dye. The absorbance of the red color, measured at 530 nm was proportional to the concentration of the sorbic acid in the sample. This automated procedure is capable of analyzing 30 samples per hour.
EFFECT OF SALT, PHOSPHATE AND SOME NONMEAT PROTEINS ON BINDING STRENGTH AND COOK YIELD OF A BEEF ROLL
Authors: MOORE S. L. , THENO D. M. , ANDERSON C. R. , SCHMIDT G. R. 
Published: August 2006

ABSTRACTBeef rolls were prepared with coarse‐ground beef (25.4 mm plate), 8% added water and either salt, salt plus 0.25% sodium tripolyphosphate (TPP), soy isolate, textured soy protein and modified whey solids at 1, 2 or 3% levels. Binding strength was measured with an Instron as the amount of force necessary to break a beef roll across bridge widths of 75, 100, 125 and 150 mm. Binding strength increased as salt content increased from 1% to 3%. Cook yield increased from 79% with 1% salt to 93% with 3% salt. The addition of 0.25% TPP resulted in an additional increase in binding strength. Cook yield increased from 93% with 1% salt plus 0.25% TPP to 98% with 3% salt plus 0.25% TPP. The modified whey selids at 2% level had the highest binding strength of the nonmeat protein materials added. This was similar to 2 or 3% added salt. The soy isolate at 3% level resulted in the highest cook yield, 78%.