Formation of Whey Protein Isolate (WPI)-Maltodextrin Conjugates in Fibers Produced by Needleless Electrospinning

被引:55
作者
Kutzli, Ines [1 ]
Gibis, Monika [1 ]
Baier, Stefan K. [2 ]
Weiss, Jochen [1 ]
机构
[1] Univ Hohenheim, Inst Food Sci & Biotechnol, Dept Food Phys & Meat Sci, Garbenstr 21-25, D-70599 Stuttgart, Germany
[2] PepsiCo Global Funct Governance & Compliance, Measurement Sci, 3 Skyline Dr, Hawthorne, NY 10532 USA
关键词
glycoconjugate; maltodextrin; whey protein isolate; Maillard reaction; needleless electrospinning; MAILLARD REACTION; PHYSICOCHEMICAL PROPERTIES; DEXTROSE EQUIVALENT; BETA-LACTOGLOBULIN; HEAT-STABILITY; GLYCATION; MALTODEXTRIN; IMPROVEMENT; GLYCOSYLATION; FUNCTIONALITY;
D O I
10.1021/acs.jafc.8b02104
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Glycation of proteins via the first stage of the Maillard reaction is capable of improving their stability but not economically feasible yet. This work reports the glycation of whey protein isolate (WPI) with maltodextrin at a high yield after heating electrospun fibers made from the reactants. Glycoconjugates were characterized by Fourier transform infrared spectroscopy (FTIR) and SDS-PAGE. The binding ratio between WPI and maltodextrin was assessed via the free amino groups. The molecular weight of the conjugates and the reaction yield were studied by size exclusion chromatography. The impact of different mass ratios between WPI and maltodextrin in the fibers (5:95, 10:90, 20:80, and 25:75 w/w) was investigated. With increasing WPI content, the binding ratio of maltodextrin decreased from,similar to 2.1 to similar to 1.2. Preferably small polysaccharides (2-13 kDa) from the maltodextrin reacted. Protein specific reaction yields of up to 44.52 +/- 7.46% w/w were demonstrated in all WPI-maltodextrin fibers after heating.
引用
收藏
页码:10283 / 10291
页数:9
相关论文
共 47 条
[1]   Whey protein-maltodextrin conjugates as emulsifying agents: An alternative to gum arabic [J].
Akhtar, Mahmood ;
Dickinson, Eric .
FOOD HYDROCOLLOIDS, 2007, 21 (04) :607-616
[2]   QUANTITATIVE STUDIES OF THE STRUCTURE OF PROTEINS IN SOLUTION BY FOURIER-TRANSFORM INFRARED-SPECTROSCOPY [J].
ARRONDO, JLR ;
MUGA, A ;
CASTRESANA, J ;
GONI, FM .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 1993, 59 (01) :23-56
[3]  
Baier S., 2013, US patent number US, Patent No. [20130264731 Al, 20130264731]
[4]   Automating a 96-Well Microtiter Plate Assay for Quick Analysis of Chemically Available Lysine in Foods [J].
Barba, Francisco J. ;
Carbonell-Capella, Juana M. ;
Esteve, Maria J. ;
Frigola, Ana .
FOOD ANALYTICAL METHODS, 2013, 6 (05) :1258-1264
[5]   Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey [J].
Bryant, CM ;
Mcclements, DJ .
TRENDS IN FOOD SCIENCE & TECHNOLOGY, 1998, 9 (04) :143-151
[6]  
Davis FJ, 2015, RSC POLYM CHEM SER, V14, P1
[7]   Food Protein-polysaccharide Conjugates Obtained via the Maillard Reaction: A Review [J].
de Oliveira, Fabiola Cristina ;
dos Reis Coimbra, Jane Selia ;
de Oliveira, Eduardo Basilio ;
Giraldo Zuniga, Abraham Damian ;
Garcia Rojas, Edwin E. .
CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION, 2016, 56 (07) :1108-1125
[8]   Emulsion stabilization by ionic and covalent complexes of beta-lactoglobulin with polysaccharides [J].
Dickinson, Eric ;
Galazka, Yanda B. .
FOOD HYDROCOLLOIDS, 1991, 5 (03) :281-296
[9]   Molecular characteristics of maltodextrins and rheological behaviour of diluted and concentrated solutions [J].
Dokic, P ;
Jakovevic, J ;
Dokic-Baucal, L .
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS, 1998, 141 (03) :435-440
[10]   Electrospinning of polymer nanofibres from multiple jets on a porous tubular surface [J].
Dosunmu, OO ;
Chase, GG ;
Kataphinan, W ;
Reneker, DH .
NANOTECHNOLOGY, 2006, 17 (04) :1123-1127