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  • 1
    Electronic Resource
    Electronic Resource
    .epsilon. Subunit of Escherichia coli F1-ATPase: effects on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysis (1987)
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 4488-4493 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00388a047
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  • 2
    Electronic Resource
    Electronic Resource
    Novel photoinduced carbon-carbon bond formation in purines (1985)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 107 (1985), S. 2183-2185 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00293a066
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  • 3
    Electronic Resource
    Electronic Resource
    Novel approaches to functionalized nucleosides via palladium-catalyzed cross coupling with organostannanes (1987)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 109 (1987), S. 7223-7224 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00257a071
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  • 4
    Electronic Resource
    Electronic Resource
    Enzymatic peptidyl .alpha.-amidation proceeds through formation of an .alpha.-hydroxyglycine intermediate (1989)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 111 (1989), S. 1933-1934 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00187a088
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  • 5
    Electronic Resource
    Electronic Resource
    DIFFERENTIAL SCANNING CALORIMETRY CAN DETERMINE KINETICS OF THERMAL DENATURATION OF BEEF MUSCLE PROTEINS (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 10 (1986), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Differential scanning calorimetry (DSC) of beef muscle produced three large endotherms occurring at 55–57°C, 65–67°C and 81–83°C. Based on earlier DSC research on isolated proteins (Privalov 1979), the concept of cooperative units participating in thermal transition phenomena was applied to beef muscle endotherms. Analysis of these endotherms by the van't Hoff relationship and Borchardt and Daniels kinetics analysis revealed reaction orders of ca. 0.6 to 2.1, 3.5 to 5.1 and 1.5 to 3.1, respectively, for the three muscle endotherms. The reaction orders for these endotherms were influenced by muscle type, fiber sarcomere length and conditioning. Aging led to an increase in reaction order whereas increased sarcomere length was accompanied by a decrease in reaction order or number of cooperative units. Changes in the number of cooperative units participating in the endotherms is discussed in the context of meat tenderization and conditioning. It appears reaction order analysis of the T3 transition (81–83°C) may correlate with meat tenderness.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1986.tb00085.x
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  • 6
    Electronic Resource
    Electronic Resource
    CHILLING INJURY. A REVIEW OF POSSIBLE MECHANISMS (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 13 (1989), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Chilling injury (CI) is a physiological defect of plants and their products that results in reduced quality and loss of product utilization following exposure to low but nonfreezing temperatures. To design more effective control strategies and maximize shelf-life, it is necessary to develop an understanding of the biochemical mechanism(s) responsible for the initiation of CI. Despite considerable efforts in this field of study, there is no general agreement on the cause or nature of CI, or even the primary event(s) triggering low temperature damage. The first unified theory to explain CI was founded on low temperature induced membrane lipid phase transitions leading to a loss of membrane integrity and physiological dysfunction. This was modified to account for the observation that the level of certain high melting phospholipids appears to be related to the chill sensitivity of many plant tissues. Membranes and changes in their physical characteristics are further implicated as having a role in CI by the discovery that chilling stress evokes an elaborate membrane retailoring response that leads to increased fluidity at reduced temperatures. Others have postulated that CI results from the direct effect of reduced temperatures on enzymes or the indirect effect of membrane perturbations on intrinsic enzymes. The redistribution of cellular calcium has most recently been advanced as the primary transducer of CI. The weight of this theory rests on the role of calcium as a secondary messenger for many cellular functions. In this review it is also speculated that lipid peroxidation may have a role in the development of irreversible injury during low temperature stress. Its effect would be similar to the senescent processes of free radical damage to tissue and progressive membrane rigidification.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1989.tb00389.x
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  • 7
    Electronic Resource
    Electronic Resource
    A REVIEW OF TEXTURAL DEFECTS IN COOKED RECONSTITUTED LEGUMES– THE INFLUENCE OF STORAGE AND PROCESSING (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food processing and preservation 9 (1985), S. 0 
    Details
    ISSN: 1745-4549
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Legumes provide an important part of the world's protein requirements, as well as other nutrients, but they are underutilized as food. A major factor limiting expanded consumption is storage induced textural defects that prolong cooking time and demand correspondingly higher energy requirements for preparation. Estimates of losses due to hardening are difficult to obtain but show the economic importance of the problem. These defects, including the hard-to-cook phenomenon and hard shell, are initiated by structural and compositional factors but can be at least partially controlled by storage and processing conditions. The available literature on bean hardening is reviewed from which it may be concluded that adverse storage conditions (high temperatures and humidities) consistently produce these defects. A kinetic approach is taken to the hardening problem, including hydration and cooking, which should allow a better understanding of the processes involved. Methods that can be utilized to produce better cooking legumes are reviewed as are processing alternatives including disruption and dry fractionation, wet fractionation, extrusion, enzymes and animal feeding. The influence of hardening on the nutritive value of legumes, although not extensively studied, is examined and it is concluded that protein quality and the availability of essential amino acids can suffer. A course of action for future research is recommended.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4549.1985.tb00716.x
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  • 8
    Electronic Resource
    Electronic Resource
    Properties and Structure of Amylose-Glyceryl Monostearate Complexes Formed in Solution or on Extrusion of Wheat Flour (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 54 (1989), 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: Differential scanning calorimetry (DSC), alpha-amylolysis, and gel filtration chromatography (GFC) were used to characterize the lamellar morphology of solution-grown amyloseglyceryl monostearate (GMS) complexes. The complexes grown at 60°C and 90°C had melting temperatures of 100°C and 114°C, respectively. Both enzyme digested complexes had broad overlapping GFC chromatographs; however, the amylose-GMS-90°C complex had chain lengths 25% to 40% larger than the lower temperature complex. Assuming the main GFC peak was representative of the ordered lamellar regions, the complexes grown at 60°C and 90°C had helical chain segments of 104 Å and 145 Å, respectively. The influence of GMS addition on the twin screw extrusion of soft wheat flour was also investigated. Formation of a complex during extrusion, characteristic of the amylose-GMS-90°C polymorph, decreased the starch solubility, water holding capacity, enzyme susceptibility and degree of expansive-puffing of the extrudate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1989.tb07920.x
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  • 9
    Electronic Resource
    Electronic Resource
    Protein Denaturation and Starch Gelatinization in Hard-To-Cook Beans (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 54 (1989), 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 study was undertaken to assess protein denaturation and starch gelatinization in ground samples of common black beans exhibiting the hard-to-cook (HTC) defect. Using differential scanning calorimetry, no significant differences in either gelatinization or denaturation temperatures were found between hard and soft beans but tropical storage conditions produced significant increases in gelatinization enthalpy and decreases in denaturation enthalpy. Endotherms of cooked samples showed as little as 34% of the protein had denatured in HTC beans as compared to over 85% in soft beans. Micrographs indicated the ground raw material was composed of clumps of cotyledon cells; cooking soft beans produced cell separation but this did not occur in HTC samples. These data supported the idea that bean hardening was accompanied by limited water availability inside cotyledon cells that could reduce cell swelling, starch gelatinization and protein denaturation, leading to textural toughness.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1989.tb05974.x
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  • 10
    Electronic Resource
    Electronic Resource
    Water-Holding Capacity in Hard-to-Cook Beans (Phaseolus vulgaris): Effect of pH and Ionic Strength (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 54 (1989), 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 effect of pH and ionic strength (IS) of soaking solution on the water holding capacity (WHC) of hard-to-cook (HTC) and control black beans (Phaseolus vulgaris) was evaluated. Beans were soaked 18 hr in solutions covering the pH range 1–7 at constant IS (1.0 M) or in solutions ranging in IS from 0.01 to 1.3M (prepared with either NaCl or CaCl2) at pH 7. WHC was significantly reduced in the pH range 3.5 to 5.1 in control beans but the effect was not as pronounced with HTC samples which had a lower WHC at each pH. Solutions prepared with NaCl produced significantly lower WHC values than CaCl2 solutions in the control but not in the HTC beans. WHC values in control beans tended to increase with higher IS, although this effect was not as apparent for HTC beans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1989.tb07950.x
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