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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 35 (1970), 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: SUMMARY— The storage life of fresh, peeled and deveined tropical shrimps at 10—12°C is extended to 10—14 and 18—21 days with 0.15 and 0.25 Mrad, respectively, as against spoilage of unirradiated samples within 4 days. Blanching treatment (steaming for 4 min) with or without brine (3.0% NaCl) extends the storage life up to 30 days at lo—12°C. the former retaining the shell-fish flavor. However, the blanched products develop musty odor and slimy texture during storage; subjected to irradiation (0.15 Mrad) these are devoid of undesirable attributes and are acceptable for 60 and 130 days, respectively, at 10—1°C and 2—4°C. Bacterial counts exceeding 108/g and high levels of TMAN and TVBN concur with spoilage of unirradiated shrimps. In contrast, low levels of TMAN and TVBN, despite high TBC, corroborate with high acceptability of radiation processed shrimps. In blanched as well as in blanched and irradiated shrimps TBC, TMAN and TVBN are low. Samples subjected to blanching only have low acceptability as against the improvement in quality by irradiation. These alterations in storage property have been discussed in the light of shifts in microflora.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 35 (1970), 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: SUMMARY— Bombay duck (Harpodon nehereus), a tropical fish, is readily susceptible to drip losses leading to textural alterations. These changes occur during storage at 0 or −20°C for 3 days and also by irradiation and storage at 0 or 10°C for 3 days. In situ denaturation of fibrillar proteins of Bombay duck occurs as evidenced by a decrease in salt-soluble proteins. Loss in extractability occurring at 0 or −20°C parallels increased drip loss, but appears to be arrested by pre-dip treatment in 10% sodium tripolyphosphate solution for 15 min. The radiation-induced drip loss also correlates with loss in the extractability at a radiation dose of 3 Mrad, but at 0.5 Mrad the drip loss occurs without appreciable decrease in the extractability. Pre-dip treatment in 10% sodium tripolyphosphate solution reduces the drip loss caused by 3 Mrad, but this is not reflected in the recovery of extractable proteins. Loss in the extractability could be attributed to the aggregation phenomenon of fibrillar proteins induced by irradiation. The radiation-induced off-odors appear to originate from the sarcoplasmic proteins.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 53 (1988), 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: Cathepsin B from the skeletal muscle of a fresh water fish Tilapia mossambica was purified 4280-fold with 9% recovery. The electrophoretic homogeneity of the preparation was established both under native and denatured conditions. The molecular weight of cathepsin B on the basis of its gel filtration profile was 23,500 daltons. The enzyme, an endopeptidase, hydrolysed Z-arg-arg-NNap and Bz-arg-NNap, with Km values of 0.57 and 3.23 mM, respectively. Cathepsin B did not display aminopeptidase activity, but cleaved Bz-arg-NH2, exhibiting the specificity of a carboxypeptidase. Among protein substrates tested, only azocoll was hydrolyzed at lower pH values. Leu-peptin, antipain and thiol blockers abolished the enzyme activity completely. The Kcat set-1 value of fish cathepsin B seemed to be lower than that of mammalian enzyme.
    Type of Medium: Electronic Resource
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  • 4
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    Unknown
    London : Periodicals Archive Online (PAO)
    Community development journal. 11:4 (1960:Sept.) 93 
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 5 (1981), S. 0 
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The interaction of malonaldehyde with lysozyme has been assessed with reference to incubation time, pH, concentration and aging. Gel filtration studies revealed that freshly prepared malonaldehyde contains a small proportion of compounds absorbing at 267 and 350 nm, which shows significant increase upon incubation of malonaldehyde. While higher concentration of malonaldehyde leads to inactivation of enzyme, lower concentration (2.5 mM) stimulates the lytic function of lysozyme. Stimulation and inactivation of the enzyme have been discussed in the context of degradation of malonaldehyde.
    Type of Medium: Electronic Resource
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