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首页> 外文期刊>Food Hydrocolloids >Structural and thermodynamic properties underlying the novel functionality of sodium caseinate as delivery nanovehicle for biologically active lipids
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Structural and thermodynamic properties underlying the novel functionality of sodium caseinate as delivery nanovehicle for biologically active lipids

机译:酪蛋白酸钠作为生物活性脂质传递纳米载体的新型功能的结构和热力学性质

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摘要

Using a combination of static and dynamic multiangle laser light scattering, various structural (the weight-average molar weight, M_w; the radius of gyration, R_G; the hydrodynamic radius, R_h: the structure-sensitive parameter, ρ = R_G/R_h: the density, d), and thermodynamic (the second virial coefficient, A_2. reflecting the nature and intensity of both the biopolymer-biopolymer and biopolymer-solvent pair interactions) parameters have been determined for the complex particles formed between sodium caseinate (SCN) and polyunsaturated soy phosphatydilcholine (PC) liposomes in an aqueous medium at the different experimental conditions (pH: 7.0, 6.0, 5.5, and the ionic strength of the buffers: 0.001 M, 0.01M, 0.1M). It was established that both the sufficiently high density (>2 mg ml~(-1)) and the specific architecture of the complex particles were the key structural properties providing the novel functionality of SCN particles as delivery vehicles for the polyunsaturated PC, in particular, as the protectors for PC against oxidation, and as the regulators of the initial velocity of the proteolysis of the complex particles under the enzymatic action in-vitro. In turn the thermodynamic affinity of the complex particles for an aqueous medium was found to be the prevailing factor in the control of such characteristic traditional functionality of SCN as the foaming ability. The data of the differential scanning calorimetry testified the maintenance of the bilayers of the phospholipid (dipalmitoylphosphatydilcholine (DPPC)) liposomes under the formation of the complex particles with the protein. Moreover, as a result of the protein-phospholipid interactions the bilayers became even more thermodynamically stable.
机译:使用静态和动态多角度激光散射的组合,各种结构(重均分子量M_w;回转半径R_G;流体动力学半径R_h:结构敏感参数ρ= R_G / R_h:已确定酪蛋白酸钠(SCN)与多不饱和脂肪酸之间形成的复合颗粒的热力学参数(第二维里系数A_2,反映了生物聚合物-生物聚合物和生物聚合物-溶剂对相互作用的性质和强度)的参数在不同实验条件(pH:7.0、6.0、5.5和缓冲液的离子强度:0.001 M,0.01M,0.1M)下,水性介质中的大豆磷脂酰胆碱(PC)脂质体。已确定足够高的密度(> 2 mg ml〜(-1))和复杂颗粒的特定结构都是关键的结构性质,提供了SCN颗粒作为多不饱和PC的输送媒介的新颖功能,特别是,作为PC的抗氧化保护剂,以及作为体外酶促作用下复杂颗粒蛋白水解初始速度的调节剂。反过来,发现复合颗粒对水性介质的热力学亲合力是控制SCN这种典型的传统功能性(如起泡能力)的主要因素。差示扫描量热法的数据证明了在与蛋白质形成复合颗粒的情况下,磷脂(双棕榈酰磷脂酰胆碱(DPPC))脂质体的双层的维持。而且,由于蛋白质-磷脂相互作用,双层变得更加热力学稳定。

著录项

  • 来源
    《Food Hydrocolloids》 |2014年第1期|149-161|共13页
  • 作者单位

    N. M. Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, Kosygin str. 4, 119334 Moscow, Russian Federation;

    N. M. Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, Kosygin str. 4, 119334 Moscow, Russian Federation;

    N. M. Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, Kosygin str. 4, 119334 Moscow, Russian Federation;

    N. M. Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, Kosygin str. 4, 119334 Moscow, Russian Federation;

    N. M. Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, Kosygin str. 4, 119334 Moscow, Russian Federation;

    N. M. Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, Kosygin str. 4, 119334 Moscow, Russian Federation;

    N. M. Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, Kosygin str. 4, 119334 Moscow, Russian Federation;

  • 收录信息 美国《科学引文索引》(SCI);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    Phosphatidylcholine liposomes; Sodium caseinate; Supramolecular complexes; Structural parameters; Protection against oxidation; Proteolysis in-vitro;

    机译:磷脂酰胆碱脂质体;酪蛋白酸钠;超分子复合物;结构参数;防止氧化;体外蛋白水解;

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