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  • 1
    Electronic Resource
    Electronic Resource
    EFFECT OF SEVERAL EXPERIMENTAL PARAMETERS ON COMBINATION OF RED KIDNEY BEAN (PHASEOLUS VULGARIS) α-AMYLASE INHIBITOR WITH PORCINE PANCREATIC α-AMYLASE (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 1 (1978), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Purified red kidney bean (Phaseolus vulgaris) amylase inhibitor forms a 1:1 stoichiometric complex with porcine pancreatic α-amylase leading to complete loss of enzyme activity on starch. Rate of complex formation is pH dependent and is maximal at pH 5. The rate constants for complex formation, as measured by loss of amylase activity, were 2.85 × 104 M-1 sec-1 at pH 6.9 (ionic strength of 0.918) and 2.55 × 105 M-1 sec-1 at pH 5 at 30°C. At pH 6.9, rate of complex formation was 4.8 times faster at 0.918 ionic strength as compared with the rate at 0.138 ionic strength. At 30°C, pH 6.9 and ionic strength of 0.168 the dissociation constant of the enzyme-inhibitor complex was determined to be 3.5 × 10-11 M. The rate constant for dissociation of the complex was calculated to be 8.7 × 10-8 sec-1 under the same conditions. The rate constant for complex formation, at ionic strength of 0.168, was 1.1 × 104 M-1 sec-1 at 370 and 9.77 × 102 M-1 sec-1 at 25.7°C. The calculated activation energy for complex formation is 39.5 kcal/mole suggesting a rate-controlling conformational change. Oxidation of the carbohydrate moiety of the glycoprotein inhibitor caused complete loss of activity. Maltose, a competitive inhibitor of α-amylase, bound as readily to the enzyme-inhibitor complex as to free α-amylase. Trypsinized α-amylase, although still able to bind to Sephadex, did not bind inhibitor. The experiments with maltose and trypsinized amylase suggest the inhibitor may not bind at the active site of α-amylase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1978.tb00184.x
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  • 2
    Electronic Resource
    Electronic Resource
    PURIFICATION AND SOME PHYSICAL AND CHEMICAL PROPERTIES OF RED KIDNEY BEAN (PHASEOLUS VULGARIS) α-AMYLASE INHIBITOR (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 1 (1978), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Red kidney bean contains more amylase inhibitor than do California white bean and cowpea while garbanzo bean and Westan and Westley lima beans do not contain inhibitor. Red kidney bean amylase inhibitor was purified to homogeneity by selective heat treatment (60°C) of a water extract at pH 4. 0, fractionation with ethanol and successive chromatography on DEAE- and CM-cellulose chromatography. The inhibitor has an apparent molecular weight of 49,000 by Sephadex gel filtration and contains 8. 6% carbohydrate probably covalently linked via an amide linkage to asparagine. The inhibitor probably contains four subunits perhaps of three different types. The inhibitor is high in aspartic acid, glutamic acid, serine, threonine and valine, low in cysteine/cystine and does not contain proline. Stable 1:1 complex formation between inhibitor and porcine pancreatic α-amylase was demonstrated by gel filtration on Sephadex G-100. The inhibitor has activity against porcine pancreatic α-amylase, human salivary α-amylase, and Tenebrio molitor (yellow corn meal worm) larval midgut α-amylase but is inactive against Bacillus subtilis α-amylase, Aspergillus oryzae α-amylase, barley α-amylase and red kidney bean α-amylase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1978.tb00183.x
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  • 3
    Electronic Resource
    Electronic Resource
    Measurement of Lipoxygenase Activity in Homogenized Green Bean Tissue (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), 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 polarographic assay was adapted to measure lipoxygenase activity in homogenized vegetable tissue. The method was verified using ground green beans. Km value, pH optimum, and rate of thermal inactivation of lipoxygenase were measured in macerated green bean seed samples and compared with published values. In general our results using homogenized samples were similar to published reports for purified green bean lipoxygenase. We observed that ionic strength, pH, and dibasic phosphate concentration must be properly controlled in the assay of lipoxygenase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1991.tb05365.x
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  • 4
    Electronic Resource
    Electronic Resource
    Plasmin Inactivation with Pulsed Electric Fields (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 60 (1995), 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: Plasmin (fibrinolysin E.C.3.4.21.7), an indigenous enzyme in bovine milk, added to simulated milk ultrafiltrate (SMUF) at 100 μg/mL (pH 6.11 and ionic strength 0.056 M) was treated at 10°C and 15°C with pulsed electric fields (HVPEF) of 15, 30 and 45 kV/cm and number of pulses 10, 20, 30, 40 and 50. The plasmin activity measured using a commercial assay, was reduced 90% after 50 pulses at both 30 and 45 kV/cm and at a processing temperature of 15°C. Similar inactivation was obtained when plasmin (100 μg/mL) in SMUF was heated at 40°C for 15 min. Inactivation of the enzyme depended on the number of pulses applied during treatment, intensity of the applied field, and processing temperature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1995.tb06310.x
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  • 5
    Electronic Resource
    Electronic Resource
    Heat Induced Gelation of Pea (Pisum sativum) Mixed Globulins, Vicilin and Legumin (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 59 (1994), 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: Mixed globulins (MG) were extracted from ground dry peas (Pisum sativum, B-160) with 0.5M NaCl, 50 mM potassium phosphate, pH 7.2, and isolated by precipitation at pH 4.5. Crude vicilin and legumin were fractionated from the MG by dialysis against 0.2M NaCl, pH 4.8, and centrifugation, then further purified using DEAE-cellulose chromatography. Conditions for maximum gel hardness of heat induced MG gel, as determined with an Instron Universal Testing Machine, were heating for 20 min at pH 7.1 at 87°C. Purified vicilin, but not legumin, formed heat induced gels. The relationship was linear between protein (globulin) concentration and log gel hardness. At all protein concentrations studied, as proportion of legumin decreased, gel hardness increased.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1994.tb05570.x
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  • 6
    Electronic Resource
    Electronic Resource
    Browning of Dehydroascorbic Acid and Chlorogenic Acid as a Function of Water Activity (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 55 (1990), 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: Browning and degradation of dehydroascorbic acid (DHA) and chlorogenic acid (CA) at pH 6, was studied at variable water activities (aw) and temperature in a model food system containing cellulose, DHA and/or CA. Rate of DHA browning followed an apparent zero order reaction and was maximum at intermediate aw. Activation energies for browning ranged from 13-17 Kcal and were independent of aw. Browning and degradation of CA was negligible at aw below 0.6. CA loss in the DHA-CA mixture was apparently delayed by decomposition products of DHA and this was pronounced at high aw.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1990.tb03950.x
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  • 7
    Electronic Resource
    Electronic Resource
    High Hydrostatic Pressure Affects Flavor-binding Properties of Whey Protein Concentrate (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 effects of high hydrostatic pressure (HHP) on flavor-binding properties of whey protein concentrate (WPC) were determined with benzaldehyde, heptanone, octanone, and nonanone. After HHP treatment (600 MPa, 50 °C, for 0-, 10-, or 30-min holding time), flavor-binding properties of WPC were studied by intrinsic fluorescence titration and static headspace analysis. The HHP treatments increased the number of binding sites and the apparent dissociation constants of WPC for benzaldehyde. HHP treatment of WPC for 0 min increased the number of binding sites of WPC for heptanone and octanone. As observed by headspace analysis, HHP treatments did not result in significant changes in the flavor retention for benzaldehyde in WPC solutions. Flavor retention of 100 ppm and 200 ppm heptanone and octanone in HHP-treated (10 min) WPC was significantly lower than for untreated WPC and HHP-treated WPC for 0 min or 30 min. For flavor retention of nonanone, significant decreases were only observed at 100 ppm when WPC solutions were HHP-treated for 10 min. While use of HHP treatment of WPC has potential in real food systems, these findings demonstrate the importance of careful selection of HHP treatment times and flavor concentrations for desired outcomes in food applications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2005.tb08308.x
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