The effect of emulsifying salts on the turbidity of a diluted milk system with varying pH and protein concentration

被引:28
作者
Culler, M. D. [1 ]
Saricay, Y. [1 ]
Harte, F. M. [1 ]
机构
[1] Penn State Univ, Dept Food Sci, University Pk, PA 16802 USA
关键词
emulsifying salt; process cheese; turbidity; micellar structure; PHYSICOCHEMICAL PROPERTIES; CASEIN MICELLES; SKIM MILK; DISSOCIATION; MICROSTRUCTURE; SCATTERING; CHEESE;
D O I
10.3168/jds.2017-12549
中图分类号
S8 [畜牧、 动物医学、狩猎、蚕、蜂];
学科分类号
0905 ;
摘要
Solutions of 10 commonly used emulsifying salts (ES) listed in the Code of Federal Regulations (21CFR133.179) for pasteurized process cheese were tested for their effect on the turbidity of a diluted milk system at different pH and protein concentrations to characterize the conditions that affect micellar structure. Emulsifying salt solutions were made by mixing the ES in a 1-in-20 dilution of water in skim milk ultra filtrate (3 kDa molecular weight cut-off) to obtain ES concentrations from 0 to 248 mM. Skim milk was added to solutions containing nanopure water, skim milk ultrafiltrate, and a specific ES ranging in concentration from 0 to 248 m.M. and pH 5, 5.8, 6.8, 7.8, and 8.8. The turbidity of the samples was measured as the optical density at 400 nm immediately after mixing (time, t = 0), after 30 s (t = 30s), and after 30 min (t = 30min). Emulsifying salts were found to cause a decrease in the turbidity of the system, which was modeled using an exponential decay model, where C* represents a threshold salt concentration at which rapid dissociation occurs. At pH values 5.8 and 6.8, the ES caused the greatest decrease in turbidity of the diluted milk system. At pH 5, the ES had the least effect on the turbidity of the system. Sodium hexametaphosphate was found to have the strongest dissociative effect, with a C* value of 0.33 mM for t = 0 at pH 6.8. In contrast, the largest C* value calculated at pH 6.8 was monosodium phosphate at 278.22 mM. Increased time resulted in lower C* values. The model established for this study can be used to predict the dissociation of casein micelles in the presence of various types of ES.
引用
收藏
页码:4241 / 4252
页数:12
相关论文
共 22 条
[1]   Heat-induced, pH-dependent dissociation of casein micelles on heating reconstituted skim milk at temperatures below 100 degrees C [J].
Anema, SG ;
Klostermeyer, H .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1997, 45 (04) :1108-1115
[2]  
[Anonymous], 2004, CHEESE CHEM PHYS MIC
[3]   Texture and microstructure of block type processed cheese with formulated emulsifying salt mixtures [J].
Awad, RA ;
Abdel-Hamid, LB ;
El-Shabrawy, SA ;
Singh, RK .
LEBENSMITTEL-WISSENSCHAFT UND-TECHNOLOGIE-FOOD SCIENCE AND TECHNOLOGY, 2002, 35 (01) :54-61
[4]   Modifications of structures and functions of caseins: a scientific and technological challenge [J].
Broyard, Camille ;
Gaucheron, Frederic .
DAIRY SCIENCE & TECHNOLOGY, 2015, 95 (06) :831-862
[5]  
CARIC M, 1985, FOOD MICROSTRUCT, V4, P297
[6]  
de Kort E., 2012, THESIS
[7]   Caseins in emulsions: interfacial properties and interactions [J].
Dickinson, E .
INTERNATIONAL DAIRY JOURNAL, 1999, 9 (3-6) :305-312
[8]   Substructure of bovine casein micelles by small-angle X-ray and neutron scattering [J].
Holt, C ;
de Kruif, CG ;
Tuinier, R ;
Timmins, PA .
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS, 2003, 213 (2-3) :275-284
[9]   Casein and casein micelle structures, functions and diversity in 20 species [J].
Holt, Carl .
INTERNATIONAL DAIRY JOURNAL, 2016, 60 :2-13
[10]   Casein interactions: Casting light on the black boxes, the structure in dairy products [J].
Horne, DS .
INTERNATIONAL DAIRY JOURNAL, 1998, 8 (03) :171-177