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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biotechnology progress 7 (1991), S. 348-354 
    ISSN: 1520-6033
    Source: ACS Legacy Archives
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 69 (2004), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Casein was hydrolyzed by trypsin to 5% degree of hydrolysis, and the hydrolysate was fractionated by ultrafiltration. While screening for the best emulsifying properties, the retentate fraction was systematically fractionated by ammonium sulfate precipitation, ion exchange, and reverse-phase high-performance liquid chromatography (HPLC). Residue from 30% ammonium sulfate saturation yielded 3 fractions on anion exchange chromatography. Preparative reverse-phase HPLC was used to isolate 4 peptides with good emulsifying properties for characterization. Computational methods were used to complement amino acid sequencing, and the peptides were identified as originating from αs-1 casein (f167-208), β-casein (f48-63), and (f129-184). A 4th peptide could not be conclusively identified. Properties of the emulsifying peptides are discussed.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 60 (1995), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Whey protein isolate (WPI) was modified to enhance foaming characteristics by controlled hydrolysis using proteolytic enzymes. Alcalase, acid fungal protease, chymotrypsin, pepsin and trypsin were used to hydrolyze 5% rehydrated WPI. Decree of hydrolvsis was estimated by freezing point depression and terminated at 2.5 to 3% by heating or pH adjustment. Controls were treated under similar conditions but without enzymes. Hydrolysates were separated into permeate and retentate by ultrafiltration and concentrated by reverse osmosis before freeze drying. Foam capacity, stability and surface tension of hydrolysates were measured. Permeate from Alcalase exhibited the best foaming characteristics, comparable to egg white.
    Type of Medium: Electronic Resource
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  • 4
    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 collaborative study involving nine laboratories was conducted over four years to evaluate a rapid, simple and reliable whipping method for measuring overrun and foam stability. Effectiveness of the method was assessed by measuring the characteristics of foams formed by three protein solutions (5%): sodium caseinate, milk protein isolate, and egg white protein; identifying and systematically eliminating sources of variability. Major sources of variability were protein dispersing technique, the mixer, and the care exercised by the operator during sampling and weighing. The method detected differences in foam stability between egg white, casein and milk protein isolate (pooled SD = 4.5) using different mixers.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 37 (1972), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Diffusion-extracted (DE) sunflower meal and protein isolate were compared with untreated samples for their nitrogen extractability and moisture adsorption. Nitrogen extractability values of 90% were found at pH 7 or above in the untreated meal, whereas a maximum solubility of only 70% was achieved at pH 9.0 in the DE meal prepared at 60°C. DE meal prepared at 80°C had low solubility over a pH range of 1–11 which indicated substantial denaturation of the sunflower proteins. The untreated isolate showed a sharp minimum solubility point in contrast to the law solubility of the DE isolate over a pH range of 3–7. Moisture adsorption values for the samples held at 5, 20 and 30°C indicated little difference in moisture contents at relative humidities of 11–55%. At higher levels, however, the untreated meal adsorbed more moisture than the DE meal. A reverse trend was noticed for the isolates as the moisture content of the DE isolate was higher than the untreated sample. The rate of moisture uptake by sunflower kernels was slower than that observed with rapeseed or soybean meats and lower total moisture contents were observed after a 4 hr soaking period.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 39 (1974), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 60 (1995), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Whey protein isolate was denatured at 85°C, pH 4.6 for 30 min to produce heat denatured whey protein isolate (HDWPI) which was hydrolyzed with trypsin, chymotrypsin, Alcalase or Neutrase to 2.8, 4.3, 6.0 or 8.0% degree of hydrolysis (DH). Analysis of freeze-dried fractions revealed a linear increase in primary amino groups, non-protein nitrogen and ash contents. Polyacrylamide gel electrophoresis showed that high and intermediate molecular weight peptides were converted to lower molecular weights with progress of hydrolysis. Differences in proteolysis patterns were observed with different enzymes. The time required to achieve equivalent hydrolysis at 1, 2, 3 or 4% enzyme/substrate ratio varied with the type of enzyme and DH.
    Type of Medium: Electronic Resource
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  • 8
    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 colaborative study was conducted to develop a rapid, simple and reliable procedure for determining the solubility of food protein products, e.g., spray-dried whey protein concentrate, sodium caseinate, egg white protein and soy protein isolate. The procedure was developed by modifying the nitrogen solubility index (NSI) procedure. Protein content and soluble protein were determined by micro-Kjeldahl or biuret procedures with standard deviations of 0.83-4.12 for all proteins except caseinate which had a value of 13.95. Although the biuret and micro-Kjeldahl procedures generally provided comparable accuracy and precision for protein content and solubility of certain proteins, the biuret procedure exhibited considerable error and variability for other proteins.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 62 (1997), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Vanilla ice cream with 8, 13 or 18% sucrose and 10, 14 or 18% butterfat was evaluated by descriptive analysis (DA) with 15 judges, instrumental texture measurements (ITM), and hedonic rating with 146 consumers. Increased sugar caused higher vanilla, almond, buttery, custard/eggy, sweetness, fatty, creamy, doughy and mouthcoating characteristics, and lower coolness, ice crystals, melt rate (ITM) and hardness (ITM). Increased fat caused higher buttery, custard/eggy and sweet flavor, fatty, creamy, doughy and mouthcoating texture, and lower color, ice crystals and melting rate (DA). Acceptability was positively related to the vanilla, creamy, fatty and milky characters, and negatively related to color, ice crystals and ITM hardness.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 63 (1998), S. 0 
    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 9% whey protein (WP) isolate solution at pH 7.0 was heat-denatured at 80°C for 30 min. Size-exclusion HPLC showed that native WP formed soluble aggregates after heat-treatment. Additions of CaCl2 (10–40 mM), NaCl (50–400 mM) or glucono-delta-lactone (GDL, 0.4–2.0%, w/v) or hydrolysis by a protease from Bacillus licheniformis caused gelation of the denatured solution at 45°C. Textural parameters, hardness, adhesiveness, and cohesiveness of the gels so formed changed markedly with concentration of added salts or pH by added GDL. Maximum gel hardness occurred at 200 mM NaCl or pH 4.7. Increasing CaCl2 concentration continuously increased gel hardness. Generally, GDL-induced gels were harder than salt-induced gels, and much harder than the protease-induced gel.
    Type of Medium: Electronic Resource
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