Succinylation of milk proteins: Influence on micronutrient binding and functional indices

被引:27
作者
Agarwal, Aanchal [1 ]
Pathera, Ashok K. [1 ]
Kaushik, Ravinder [2 ]
Kumar, Naveen [3 ]
Dhull, Sanju B. [4 ]
Arora, Sumit [5 ]
Chawla, Prince [1 ,6 ]
机构
[1] Shoolini Univ, Sch Bioengn & Food Technol, Solan 173229, Himachal Prades, India
[2] Amity Univ, Amity Inst Food Technol, Noida 201313, Uttar Pradesh, India
[3] Amity Univ Rajasthan, Amity Inst Biotechnol, Jaipur 303002, Rajasthan, India
[4] Chaudhary Devi Lal Univ, Dept Food Sci & Technol, Sirsa 125055, Haryana, India
[5] Natl Dairy Res Inst, Dairy Chem Div, Karnal 132001, Haryana, India
[6] Lovely Profess Univ, Sch Agr, Dept Food Technol & Nutr, Phagwara 144411, Punjab, India
关键词
Milk proteins; Succinylation; Sodium caseinate; Minerals; Vitamins; Micronutrient binding; SODIUM CASEINATE-VITAMIN; PHYSICOCHEMICAL CHARACTERIZATION; IRON; ZINC; BIOAVAILABILITY; BOVINE; CALCIUM; COMPLEX; ACID; BIOACCESSIBILITY;
D O I
10.1016/j.tifs.2020.01.016
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The functionality of milk proteins is an important feature used in food industries. Milk proteins are effectively capable of binding divalent metal ions electrostatically. As well, the hydrophobic and hydrophilic domains present in milk proteins make them excellent modules for the site-specific delivery of various bioactive analytes. Apart from vital functional properties, solubility and stability of milk proteins is always a matter of concern. To achieve the potential functional properties and micronutrient binding ability succinylation of proteins gained candidature of interest. Succinylation of milk proteins improves cellular mineral absorption during simulated gastrointestinal and transwell assay, respectively. Succinylation of various types of milk protein concentrates results in improved functional properties and micronutrient binding abilities. In the present review, functional properties, mineral and vitamin binding properties of milk proteins and their fractions are represented in detail along with the influence of the succinylation upon the respective properties of milk proteins and their fractions.
引用
收藏
页码:254 / 264
页数:11
相关论文
共 95 条
  • [1] Effect of succinylation on the physicochemical properties of soy protein hydrolysate
    Achouri, A
    Zhang, W
    [J]. FOOD RESEARCH INTERNATIONAL, 2001, 34 (06) : 507 - 514
  • [2] [Anonymous], INT J DAIRY TECHNOL
  • [3] [Anonymous], INT DAIRY FED B
  • [4] BAUMY JJ, 1988, LAIT, V68, P409, DOI 10.1051/lait:1988426
  • [5] Binding sites of retinol and retinoic acid with serum albumins
    Belatik, A.
    Hotchandani, S.
    Bariyanga, J.
    Tajmir-Riahi, H. A.
    [J]. EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY, 2012, 48 : 114 - 123
  • [6] BOUHALLAB S, 1991, LAIT, V71, P435
  • [7] Binding of vitamin A with milk α- and β-caseins
    Bourassa, P.
    N'soukpoe-Kossi, C. N.
    Tajmir-Riahi, H. A.
    [J]. FOOD CHEMISTRY, 2013, 138 (01) : 444 - 453
  • [8] Modifications of structures and functions of caseins: a scientific and technological challenge
    Broyard, Camille
    Gaucheron, Frederic
    [J]. DAIRY SCIENCE & TECHNOLOGY, 2015, 95 (06) : 831 - 862
  • [9] BRULE G, 1982, LAIT, V62, P323, DOI 10.1051/lait:1982617-62021
  • [10] Carr A.J., 2003, Advanced Dairy Chemistry Volume 1: Proteins, V1, P1289