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  • 1
    ISSN: 1745-4530
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Capacitive (Radio Frequency) dielectric heating has great potential for achieving rapid and uniform heating patterns in foods, providing safe, high quality food products. This review describes and discusses the major technology behind capacitive (RF) dielectric heating in food processing and preservation, the current applications of the technology in the industry, the potential use of mathematical modeling for heating system design, and the major challenges facing the use of this technology in food processing. A vast amount of work is still necessary to further understand the dielectric properties of both food and packaging materials in order to refine system design and maximize performance of this technology in the field of packaged food products. Various economic studies will also play an important role in understanding the overall cost and viability of commercial application of this technology in food processing.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Heat-induced denaturation of water-leached fish muscle proteins, as affected by addition of sucrose and/or salt, were investigated by differential scanning calorimetry (DSC). Net enthalpic changes for these muscle proteins were always endothermic in nature, and of a greater magnitude at faster heating rates. This was interpreted to infer that aggregation at lower heating rates led to formation of a gel structure in which potential bondings were more completely accomplished; that is, a more energetically favorable structure was attained with slow heating. The stabilization of proteins by sucrose, and destablization of proteins by salt, were revealed by shifts in transition peaks and activation energies, the latter determined by two methods of kinetic analysis.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The protein solubility and molecular-weight distribution of freeze-dried sarcoplasmic proteins (SPs) from rockfish treated under low and high pH as well as various NaCl concentrations were elucidated. The solubility of SPs was significantly suppressed at an acidic pH (2.0–4.0) and in the presence of high salt concentration (0.5 M NaCl). The least amount of protein was lost when SPs were treated at pH 2.0 or 3.0 followed by precipitation at pH 5.5. The interaction of SPs with Alaska pollock surimi (myofibrillar proteins) was also investigated. The addition of SPs appeared to delay the thermal denaturation of myosin and actin. The SPs positively contributed to the gelation of myofibrillar proteins as judged by breaking force.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Biochemical characteristics of Pacific whiting muscle proteins extracted at acidic, neutral and alkaline conditions were investigated as affected by various ionic strength levels. The protein solubility at pH 4 declined, as NaCl was added up to 200 mM, due to protein aggregation through hydrophobic interactions. In contrast, at pH 7 and 10, solubility increased as NaCl was added up to 400 mM after which it remained constant. Changes in total SH content and Sowere highly related to the different molecular weight distributions of the soluble proteins. At pH 4, myosin heavy chain (MHC) was soluble as evidenced by the presence of MHC in the soluble fraction, even though degraded molecules were shown at IS 10–100 mM, and became completely insoluble at IS ≥ 150 mM. At pH 10, the density of the MHC band gradually increased as IS increased and the formation of high MW polymers was observed at IS ≥ 150 mM.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: This study was conducted to better understand biochemical changes of fish muscle proteins as affected by novel surimi process, acid- or alkali-aided solubilization. At 10 mM NaCl, between pH 5 and 10, the solubility of Pacific whiting muscle proteins was low but increased dramatically as the pH was shifted to either acidic or alkaline pH. At 600 mM NaCl, the isoelectric point was shifted to the acidic direction by about 2 pH units, resulting in aggregation of proteins at low pH, but improving the solubility of MHC (myosin heavy chain) between pH 6 and 10. ANS surface hydrophobicity (ANS-SO) showed much greater values than PRODAN surface hydrophobicity (PRODAN-SO) for samples treated at pH 2 - 4 perhaps due to an enhancement of the electrostatic interactions between the ANS probe and proteins. At very high pH, according to hydrophobicity results, proteins were partially refolded when the ionic strength increased. Under acidic conditions, SDS-PAGE demonstrated the degradation of MHC at 10 mM NaCl. The formation of MHC polymers was observed under alkaline treatment with a concomitant decrease of SH content.
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  • 6
    ISSN: 1745-4530
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Degradation kinetics of whiting surimi gel texture were examined over a temperature/time range (40–85C, 0.5–35 min). Changes in textural properties of whiting surimi gel were mainly affected by proteolytic activity of endogenous proteinase. A decrease of failure shear stress and shear strain followed first order kinetics. The kinetic parameters developed using either isothermal or nonisothermal principles were similar. Degradation rate of gel texture increased with temperature, reaching a maximum at 55C. It then decreased to a minimum at 70C. Ea values for the activation and inactivation temperature range were 138.6–162.6 and 13.5–35.0 kJ/mol, respectively.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Total aerobic plate count (APC), shear stress, shear strain, and color of fresh Pacific whiting surimi stored at 5°C were determined at day 0, 1, 3, 5, and 7. Frozen surimi was prepared with four levels of cryoprotectams (0, 3, 6, and 9%) and was compared with fresh surimi for gelforming ability. Fresh Pacific whiting surimi had a shelf life of 5 days. The gel functionality remained unchanged throughout the storage time. Strain values of fresh surimi were not different from those of frozen surimi with 9% cryoprotectants, but stress values of fresh surimi were almost three times higher than those of frozen surimi.
    Type of Medium: Electronic Resource
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  • 8
    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: Freeze-induced protein denaturation of pollack surimi was investigated as affected by the addition of sugar and/or polyol, including a starch hydrolysate product, and/or phosphates during 8 months frozen storage. Polydextrose® appeared to substitute for the sucrose/sorbitol now used in surimi manufacture without changes in cryoprotective effect. The maltodextrin adversely affected gel-forming properties, although it maintained the salt-soluble protein extractability nearly as well as did sucrose/sorbitol or Polydextrose®. The cryoprotective effects of phosphate addition seemed to depend upon the pH and/or specific phosphate ion used.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), 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: Stabilization of fish myofibrils was investigated with respect to freeze-and heat-induced denaturation as affected by the addition of phosphates (0.25, 0.5% of sodium tripolyphosphate or neutralized pyrophosphate), alone or in combination with 8% Polydextrose® or a sucrose/sorbitol mixture. Freeze-induced aggregation was reduced effectively by combination of phosphates and carbohydrates, and, less effctively, by phosphates or carbohydrates alone. The most effective treatment consisted of 0.5% of either phosphate treatment combined with either carbohydrate treatment. Differential scanning calorimetric studies revealed that phosphate addition induced stabilization of myosin and carbohydrate addition generally induced a one-step denaturation process for myosin. No differences due to phosphate type were observed in any measured parameter.
    Type of Medium: Electronic Resource
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  • 10
    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: Pacific whiting surimi paste was ohmically heated to investigate degradation of myosin heavy chain (MHC) caused by endogenous proteinase over a range of 40–85°C and 0.5–35 min. Degradation was best described with an apparent reaction order of 1.4. Changes of degradation rate increased with temperature and reached a maximum at 57°C. Then, rate of MHC degradation decreased with higher temperature and reached a minimum at 75°C. Ea values of activation and inactivation zone were 142.3 and 83.1 kJ/mol, respectively. Generally, failure shear stress and shear strain increased linearly with MHC content. Proteolytic degradation of actin exhibited the same trend as that of MHC but at a slower rate. The synergistic effect of actin in the gelation of whiting surimi was predominant at ≥75°C.
    Type of Medium: Electronic Resource
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