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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 68 (2003), 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: : Survival analysis concepts to be used in sensory shelf life studies were introduced, together with the equations necessary for calculations. The survival function was defined as the probability of consumers accepting a product beyond a certain storage time. Censoring phenomena, a key concept in survival analysis, was defined and has been shown to occur in sensory shelf-life data. Concepts and calculations were applied to a data set obtained from 50 consumers who each tasted seven yogurt samples with different storage times, answering “yes” or “no” to whether they would consume the samples. From this censored data set, nonparametric and parametric models were obtained that allowed shelf-life estimations.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), 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: : The recovery of myofibrillar protein from beef heart using nonthermal acidic solubilization was evaluated. Postmortem time, 3 or 24 h, did not affect protein solubility (p 〉 0.05). Protein solubility and yield were detrimentally affected by salt addition. Recovery of extracted protein (yield) was maximized with 0 mM NaCl (60.8 ± 3.9%). SDS-PAGE confirmed myosin solubilization below pH 5 and suggested reduced protein solubility below pH 2.5. Extracted protein from beef heart was significantly lower in fat, cholesterol, ash, and total collagen. In addition, the protein profile using a 7% SDS-Page gel consisted mainly of heavy chain myosin (36%), 150 kDa proteins (15%), and actin (21%).
    Type of Medium: Electronic Resource
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