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  • Articles  (29,324)
  • Nature Publishing Group  (25,065)
  • Institute of Physics  (3,369)
  • Blackwell Publishing Ltd  (890)
  • 2005-2009  (17,479)
  • 1940-1944  (11,845)
  • Medicine  (27,189)
  • Process Engineering, Biotechnology, Nutrition Technology  (2,135)
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  • Articles  (29,324)
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  • 1
    Electronic Resource
    Electronic Resource
    Optimization of Thermal Pretreatment Conditions for the Separation of Native α-Lactalbumin from Whey Protein Concentrates by Means of Selective Denaturation of β-Lactoglobulin (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : In this study a method to obtain native α-lactalbumin with a high degree of purity of 98% (m/m) and recovery of 75% (m/m) by selective denaturation of β-lactoglobulin was developed. To achieve this goal, the thermal pretreatment of whey protein concentrate was optimized varying the composition of the liquid whey protein concentrate in terms of total protein, lactose and calcium content, and pH value. The kinetics of the thermal denaturation of α-la and β-lg were then investigated at predetermined optimal composition (protein content 5 to 20 g/L, lactose content 0.5 g/L, calcium content 0.55 g/L, and pH 7.5). Using the activation energies and reaction rate constants obtained, lines of equal effects for targeted denaturation degrees of α-la and β-lg were calculated. Depending on total protein content, an area of optimal heating temperature/time conditions was identified for each protein concentration level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb08319.x
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  • 2
    Electronic Resource
    Electronic Resource
    Lipid Oxidation in Microsomal Fraction of Squid Muscle (Loligo peali) (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Frozen squid is susceptible to both lipid oxidation and yellow/brown discoloration during frozen storage. The involvement of lipid oxidation in the microsomal fraction of squid muscle on oxidative rancidity and discoloration was investigated using iron and either enzymatic or non-enzymatic redox cycling pathways. Lipid oxidation was measured by thiobarbituric acid-reactive substances (TBARS), and color changes were measured spectrophotometrically using an integrating sphere. The lipid oxidation was not observed in the squid microsomes in the presence of Fe3+ and β-nicotinamide adenine dinucleotide disodium salt (NADH) or β-nicotinamide adenine dinucleotide phosphate, reduced (NADPH), suggesting that the enzymatic redox cycling pathway was not active. Iron-promoted TBARS formation was observed in the non-enzymatic pathway when ascorbic acid was used as a reducing compound. Non-enzymatic lipid oxidation increased with increasing temperature (4 °C to 37 °C), iron (0 to 100 μM), and ascorbic acid (0 to 200 μM) concentrations. As lipid oxidation in the microsomes or isolated microsomal lipids increased, color changes were observed as could be seen by an increase in b* values (yellowness) and a decrease in a* (redness) values. The ability of iron and ascorbate to promote both lipid oxidation and pigment formation in the microsomal fraction suggests that this pathway could be responsible for quality deterioration of squid muscle during storage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb11504.x
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  • 3
    Electronic Resource
    Electronic Resource
    The Effective Methods in Refolding and Activation of Cathepsin L-like Soybean Protease D3 (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A novel cysteine protease D3, which was purified from germinating soybean cotyledons, showed high homology with cathepsin L and cathepsin K. In our previous study, because of the specificity of the enzyme, hydroly-sates treated with D3 treatment showed a prominent property of less bitterness than other hydrolysates treated with commercially available proteases. However, active recombinant D3 prepared from Escherichia coli inclusion bodies was so intricate and less productive that it made further studies on this protease and hydrolysates difficult. In the concrete, the refolding process of the immature proD3 from inclusion bodies takes more than a day, and autocatalytic activation of refolded immature proD3 at low pH was difficult to control. In this study, we aimed to establish an efficient refolding and activating method of protease D3. In the refolding step, the procedures could be simplified by using a size-exclusive column-based method. In the activation step from immature proD3, we utilized another protease, subtilisin, rather than autocatalytic activation by D3 itself. After subtilisin treatment, the peptide having 12 amino acids-length of N-terminal pro sequence was initially cleaved, and residual proD3 showed only a half proteolytic activity of active D3. However, when the pH was shifted lower (pH4.5), D3 automatically changed to have the same proteolytic activity as active one, and this activated recombinant had the same N-terminal sequence as purified D3 from germinating soybean cotyledons. By using this method, all preparation processes of D3 from inclusion bodies to active D3 could be completed within a few hours, and it became possible to carry out the investigation on hydrolysates on a large scale.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb11507.x
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  • 4
    Electronic Resource
    Electronic Resource
    Detection of Fecal Contamination on Cantaloupes Using Hyperspectral Fluorescence Imagery (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: To determine whether detection of fecal contamination on cantaloupes is possible using fluorescence imaging, hyperspectral images of cantaloupes artificially contaminated with a range of diluted bovine feces were acquired from 425 to 774 nm in responses to ultraviolet-A (320 to 400 nm) excitation. Evaluation of images at emission peak wavelengths indicated that 675 nm exhibited the greatest contrast between feces contaminated and untreated surface areas. Two-band ratios compared with the single-band images enhanced the contrast between the feces contaminated spots and untreated cantaloupe surfaces. The 595/655-nm, 655/520-nm, and 555/655-nm ratio images provided relatively high detection rates ranging from 79% to 96% across all feces dilutions. However, both single band and ratio methods showed a number of false positives caused by such features as scarred tissues on cantaloupes. Principal component analysis (PCA) was performed using the entire hyperspectral images data; 2nd and 5th principal component (PC) image exhibited differential responses between feces spots and false positives. The combined use of the 2 PC images demonstrated the detection of feces spots (for example, minimum level of 16-μg/mL dry fecal matter) with minimal false positives. Based on the PC weighing coefficients, the dominant wavelengths were 465, 487, 531, 607, 643, and 688 nm. This research demonstrated the potential of multispectral-based fluorescence imaging for online applications for detection of fecal contamination on cantaloupes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb11517.x
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  • 5
    Electronic Resource
    Electronic Resource
    Ultrastructural Variation in Beef M. longissimus dorsi as an Explanation of the Variation in Beef Tenderness (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : The objective of this experiment was to quantify variation in bovine M. longissimus dorsi tenderness and determine the extent such variation is explained by variation in the ultrastructure of muscles after different postmortem treatments. Eight muscles were hot-boned and aged for 2 d at 2 °C (T1) to achieve very contracted actomyosin crossover and tough beef. Eight carcass sides were tenderstretched for 10 h at 10 °C and a further 38 h at 2 °C (T2) to achieve lengthened actomyosin crossover and tender beef. Both T1 and T2 were compared with conventionally hung carcasses, which underwent similar chilling regimes, C1 (n= 8) and C2 (n= 8), respectively. Measurements of sarcomere length, pH, Warner Bratzler shear force (WBSF), and sensory tenderness were taken, and transmission electron microscopy images analyzed. Variances of attributes were analyzed on Bartlett's test. Variances of the 4 groups were homogenous for all attributes except for pH after 24 h postmortem (with T1 [0.00] having lower variances than C1 = 0.04, T2 = 0.06, and C2 = 0.05) and WBSF after 2 d aging (with T2 [74.33] having lower variances than T1 = 236.76, C1 = 398.82, and C2 = 856.74). The variation in the tenderness of beef was quantified through ultrastructural variation in bovine muscle, with tenderstretched moderately chilled beef having the least variable tenderness as a result of more uniform overlap between actin and myosin filaments. Variation in the eating quality of beef was not reduced by hot-boning with fast chilling or conventional hanging with fast or moderate chilling. The development of the uniformity within filaments of tenderstretched muscle requires further analysis as residual variation remains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb08322.x
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of Irradiation on Microbial Safety and Nutritional Quality of Minimally Processed Bitter Gourd (Momordica charantia) (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : The feasibility of gamma radiation in combination with low temperature was studied to ensure microbiological safety and maintaining physicochemical and sensory characteristics of minimally processed bitter gourd. Radio sensitivity (D10 values, that is, irradiation dose required for 90% reduction of microorganisms) for Salmonella paratyphae A and Escherichia coli were 0.28 kGy and 0.23 kGy, respectively. On the basis of D10 values, 5D10 values were determined and samples of minimally processed bitter gourd were irradiated up to 5D10 values, stored for 14 d at 5 ± 1 °C, and analyzed for total bacterial, fungal, and coliform counts. Ascorbic acid, acidity, texture, and sensory qualities were also studied. Results showed that an irradiation dose of 2.0 kGy significantly reduced the microbial count to keep the samples microbiologically safe for 7d. Sensory evaluation revealed that the samples received maximum scores for appearance and flavor (7.8 and 7.9, respectively) with radiation dose of 2.0 kGy and minimum score for control (6.5). Firmness and ascorbic acid content decreased significantly with increase in storage time and irradiation dose. All the samples were discarded during the 2nd wk of storage due to high bio-burden.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb09980.x
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  • 7
    Electronic Resource
    Electronic Resource
    Crystallization and X-ray Diffraction of Crystals Formed in Water-Plasticized Amorphous Spray-dried and Freeze-dried Lactose/Protein Mixtures (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Effects of proteins (whey protein isolate [WPI], Na-caseinate, and gelatin), drying method, storage relative vapor pressure (RVP), and time on lactose crystallization and crystals formed were investigated using x-ray diffraction (XRD). Crystallization was observed from increasing peak intensities of XRD patterns. Lactose in lactose/protein (5:1,3:1) mixtures crystallized in samples stored at RVP of 44.1% and above in both spray-dried and freeze-dried materials, except in freeze-dried lactose/Na-caseinate and lactose/gelatin mixtures, which showed lactose crystallization at 54.5% RVP and above. The rate of crystallization increased with increasing RVP and storage time. The rate of crystallization in spray-dried materials was higher than in freeze-dried materials, and the crystallization rate decreased with increasing protein content. Lactose crystallized mainly as α-lactose monohydrate in spray-dried lactose/WPI and lactose/gelatin mixtures. Crystals formed in freeze-dried lactose/WPI and lactose/gelatin mixtures were anhydrous β-lactose and α-lactose monohydrate crystals. Lactose crystallized as a-lactose monohydrate in both spray-dried and freeze-dried lactose/Na-caseinate mixtures. Trace amounts of anhydrous β-lactose were present in spray-dried lactose/WPI (5:1) and lactose/gelatin (5:1) mixtures. Peak intensities of XRD patterns for anhydrous β-lactose decreased with increasing protein content and storage time. The crystallization data were successfully modeled using Avrami equation at an RVP of 65.6% and above. These data are important in understanding and predicting storage stability of lactose- and protein-containing food and pharmaceutical materials.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb09977.x
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  • 8
    Electronic Resource
    Electronic Resource
    A Continuous High Pressure Carbon Dioxide System for Microbial Reduction in Orange Juice (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : A continuous high-pressure carbon dioxide system, run at ambient conditions, was tested on its performance in reducing both natural and inoculated microbial loads. The prototype system continuously processes orange juice with carbon dioxide (CO2) at high pressures. A central composite design was originally used to examine the variables of pressure, residence time, and CO2/juice ratio. For microbial reduction, residence time was the major factor followed by pressure. The CO2/juice ratio showed no influence on microbial load, and in this equipment, was difficult to control. The unit was able to cause a 5-log reduction of the natural flora in spoiled juice, and could attain a 5-log decrease in numbers of pathogenic Escherichia coli O157:H7, Salmonella typhimurium, and Listeriamonocytogenes. No viable cells of E. coli O157:H7 orS. typhimurium were cultured after the treated juices were stored at room temperature (22 °C) for 14 d. Thus, non-thermal pathogen reduction is possible with this system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb09979.x
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  • 9
    Electronic Resource
    Electronic Resource
    Biosynthesis of 1-Octen-3-ol and 10-Oxo-trans -8-decenoic Acid Using a Crude Homogenate of Agaricus bisporus: Reaction Scale Up (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : The enzymatic reaction that produces 1 -octen-3-ol and 10-oxo-trans-8-decenoic acid was successfully scaled up from a 1 -L to a 10-L bioreactor using a crude mushroom homogenate of Agaricus bisporus. For this non-Newtonian reaction broth, the agitation rate was considered the most important controlling factor for the scale up. An agitation rate of 600 rpm, for an aeration rate of 0.44 m3/m3/h, was found to be the minimum to maintain the yield constant for the 1-L reactor. Subsequently, the agitation rate for the 10-L reactor was determined using 2 different approaches: a constant power per volume of liquid and a constant volumetric mass transfer coefficient (kLa). The constant power per volume of liquid approach predicted an agitation rate of 364 rpm that resulted in being too low to maintain the same yield obtained with the 1-Lreactor. Measurement of the kLa for the 10-Lreactor, at 364 rpm and an aeration of 0.44 m3/m3/h, produced a value of 11.7/h, thus confirming that the reaction in the larger reactor was oxygen-deprived. Therefore, the use of constant volumetric mass transfer coefficient (kLa) strategy was used instead. kLa was experimentally determined at different agitation rates for the 10-L reactor. It was found that 750 rpm produced a kLa of 40.2/h. Confirmatory reactions were run in both reactors with the same batch of mushrooms, and the results were equivalent, thus indicating that was a good criterion for scaling up this process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb09978.x
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  • 10
    Electronic Resource
    Electronic Resource
    Optimization of Incorporated Prebiotics as Coating Materials for Probiotic Microencapsulation (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 70 (2005), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : The purpose of this research was to improve probiotic microencapsulation using prebiotics and modern optimization techniques to determine optimal processing conditions, performance, and survival rates. Prebiotics (fructooligosaccharides or isomaltooligosaccharides), growth promoter (peptide), and sodium algi-nate were incorporated as coating materials to microencapsulate 4 probiotics (Lactobacillus acidophilus, Lacto-bacillus casei, Bifidobacterium bifidum, and Bifidobacterium longum). The proportion of the prebiotics, peptide, and sodium alginate was optimized using response surface methodology (RSM) to 1st construct a surface model, with sequential quadratic programming (SQP) subsequently adopted to optimize the model and evaluate the survival of microencapsulated probiotics under simulated gastric fluid test. Optimization results indicated that 1% sodium alginate mixed with 1% peptide and 3% fructooligosaccharides as coating materials would produce the highest survival in terms of probiotic count. The verification experiment yielded a result close to the predicted values, with no significant difference (P 〉 0.05). The storage results also demonstrated that addition of prebiotics in the walls of probiotic microcapsules provided improved protection for the active organisms. These probiotic counts remained at 106 to 107 colony-forming units (CFU)/g for microcapsules stored for 1 mo and then treated in simulated gastric fluid test and bile salt test.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb09981.x
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