Textural Properties of Beta-lactoglobulin Sodium Alginate Mixed Gels at Large Scale Deformation

被引:1
|
作者
Haug, I. J. [1 ]
Carlsen, A. -M. H. [1 ]
Vegarud, G. E. [2 ]
Langsrud, T. [2 ]
Draget, K. I. [1 ]
机构
[1] Norwegian Univ Sci & Technol NTNU, Inst Biotechnol, Norwegian Biopolymer Lab NOBIPOL, N-7491 Trondheim, Norway
[2] Norwegian Univ Life Sci UMB, Inst Chem Biotechnol & Food Sci IKBM, As, Norway
关键词
beta-lactoglobulin; denaturation; DSC; mechanical properties; small-and large deformation measurements; sodium-alginate; THERMAL-DENATURATION; RHEOLOGICAL PROPERTIES; GELATION; AGGREGATION; PROTEINS;
D O I
10.1111/j.1745-4603.2012.00365.x
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The denaturation and gelling properties of mixed systems of -lactoglobulin and sodium-alginate have been investigated as a function of alginate molecular weight, chemical composition, concentration, pH and ionic strength. Differential scanning calorimetry and small strain oscillatory measurements showed that denaturation temperature were lower than the gelling temperatures under the conditions examined. The denaturation temperatures were dependent on both pH and ionic strength, but unaffected by alginate concentration and type. The mechanical and textural properties of mixed gels of -lactoglobulin and sodium alginate were dependent on several factors; the gel strength increased as a function of alginate concentration under ambient conditions, and decreased as the pH and/or the ionic strength were changed. High molecular weight alginate gave the most pronounced effects, probably due to the accessibility of the alginate for protein binding. The chemical composition of the alginate had negligible effect on the mechanical properties of the gels. Practical Applications As both proteins and polysaccharides are widely used in the food industry, it is important to understand the interactions between these two biopolymers in order to envisage final product properties. The present article gives an overview of several important parameters when mixing -lactoglobulin and sodium alginate. -Lactoglobulin is the main protein in whey and one of the major food protein ingredients. Alginate is a polysaccharide that is often used in the food industry because of its functional properties. This study shows that if the conditions and the alginate type are adequately chosen, the textural properties of food products can be controlled and tailored.
引用
收藏
页码:56 / 65
页数:10
相关论文
共 50 条
  • [21] Textural, mechanical, and microstructural properties of restructured pimiento alginate-guar gels
    Mousavi, Seyyed Mohammad Reza
    Rafe, Ali
    Yeganehzad, Samira
    JOURNAL OF TEXTURE STUDIES, 2019, 50 (02) : 155 - 164
  • [22] Modification of the structural and rheological properties of β-lactoglobulin/κ-carrageenan mixed gels induced by high pressure processing
    Li, Xiaoying
    He, Xiaoye
    Mao, Like
    Gao, Yanxiang
    Yuan, Fang
    JOURNAL OF FOOD ENGINEERING, 2020, 274
  • [23] MERCAPTOETHANOL, N-ETHYLMALEIMIDE, PROPYLENE-GLYCOL AND UREA EFFECTS ON RHEOLOGICAL PROPERTIES OF THERMALLY INDUCED BETA-LACTOGLOBULIN GELS AT ALKALINE PH
    MULVIHILL, DM
    RECTOR, D
    KINSELLA, JE
    JOURNAL OF FOOD SCIENCE, 1991, 56 (05) : 1338 - 1341
  • [24] Structural features of transiently modified beta-lactoglobulin relevant to the stable binding of large hydrophobic molecules
    Lozinsky, Evgenia
    Iametti, Stefania
    Barbiroli, Alberto
    Likhtenshtein, Gertz I.
    Kalai, Tamas
    Hideg, Kalman
    Bonomi, Francesco
    PROTEIN JOURNAL, 2006, 25 (01) : 1 - 15
  • [25] Time and temperature aspects of beta-lactoglobulin removal from methylated silica surfaces by sodium dodecyl sulphate
    Karlsson, CAC
    Wahlgren, MC
    Tragardh, AC
    COLLOIDS AND SURFACES B-BIOINTERFACES, 1996, 6 (4-5) : 317 - 328
  • [26] THERMAL-DENATURATION AND HEAT-INDUCED GELATION PROPERTIES OF BETA-LACTOGLOBULIN - EFFECTS OF SOME CHEMICAL-PARAMETERS
    LIU, TX
    RELKIN, P
    LAUNAY, B
    THERMOCHIMICA ACTA, 1994, 246 (02) : 387 - 403
  • [27] Unraveling the effects of low protein-phenol binding affinity on the structural properties of beta-lactoglobulin
    Schild, Kerstin
    Soennichsen, Frank D.
    Martin, Dierk
    Garamus, Vasil M.
    Van der Goot, Atze Jan
    Schwarz, Karin
    Keppler, Julia K.
    FOOD CHEMISTRY, 2023, 426
  • [28] BETA-LACTOGLOBULIN BINDING-PROPERTIES DURING ITS FOLDING CHANGES STUDIED BY FLUORESCENCE SPECTROSCOPY
    DUFOUR, E
    GENOT, C
    HAERTLE, T
    BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1994, 1205 (01): : 105 - 112
  • [29] An exploration of the interaction, structural characterization and anti-oxidative properties of proanthocyanidin and beta-lactoglobulin complex
    Duan, Cuicui
    Qin, Mengchun
    Liu, Lifan
    Sun, Yixue
    Cai, Lin
    Ma, Lin
    Li, Xiaolei
    Ma, Fumin
    Li, Dan
    FOOD RESEARCH INTERNATIONAL, 2025, 202
  • [30] Design and characterization of double-cross-linked emulsion gels using mixed biopolymers: Zein and sodium alginate
    Yan, Jun
    Liang, Xiuping
    Ma, Cuicui
    McClements, David Julian
    Liu, Xuebo
    Liu, Fuguo
    FOOD HYDROCOLLOIDS, 2021, 113