Effect of pulsed light treatment on structural and functional properties of whey protein isolate

被引：75

作者：

Siddique, Md Abu Bakar ^{[1
]}

Maresca, Paola ^{[2
]}

Pataro, Gianpiero ^{[1
]}

Ferrari, Giovanna ^{[1
,2
]}

机构：

[1] Univ Salerno, Dept Ind Engn, Via Giovanni Paolo 2, I-84084 Fisciano, SA, Italy

[2] ProdAl Scarl, Via Ponte Melillo, I-84084 Fisciano, SA, Italy

来源：

FOOD RESEARCH INTERNATIONAL | 2016年 / 87卷

关键词：

Pulsed light; Whey protein; Unfolding; Solubility; Foaming properties; Conformational structure; BETA-LACTOGLOBULIN; THERMAL-DENATURATION; FOAMING PROPERTIES; EGG-WHITE; PHYSICOCHEMICAL PROPERTIES; ALPHA-LACTALBUMIN; HEAT-TREATMENT; SKIM MILK; PH; AGGREGATION;

D O I：

10.1016/j.foodres.2016.07.017

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

This work aimed at investigating the effects of Pulsed Light (PL) processing at different fluences (from 4 to 16 J/cm(2)) on the structure and functional properties of Whey Protein Isolate (WPI) solution. The determination of the free and total sulfhydryl (SH) groups was used to detect the variation of WPI tertiary and quaternary structure. Additionally, PL-induced changes in secondary structure were determined by FT-IR spectroscopy and the differential scanning calorimetry (DSC), and primary structure by carbonyl content The experimental data demonstrated that PL treatments increased the concentration of total and free sulfhydryl groups and protein carbonyls. A decrease of the denaturation temperature and enthalpy ratio with increasing the intensity of PL treatments was observed in DSC measurements. Small but significant changes in the secondary structure of PL treated WPI solution were also taking place and detected. The extent of whey protein structure modifications was fluence dependent. The results of this investigation demonstrated the potential of PL treatments to induce dissociation and partial unfolding of WPI, thus improving some of their functional properties, such as solubility and foaming ability. (C) 2016 Elsevier Ltd. All rights reserved.

引用

页码：189 / 196

页数：8

共 54 条

[1] DETERMINATION OF SH-GROUPS AND SS-GROUPS IN SOME FOOD PROTEINS USING ELLMANS REAGENT [J].

BEVERIDGE, T ;

TOMA, SJ ;

NAKAI, S .

JOURNAL OF FOOD SCIENCE, 1974, 39 (01) :49-51

[2] Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin:: a differential scanning calorimetric study [J].

Boye, JI ;

Alli, I .

FOOD RESEARCH INTERNATIONAL, 2000, 33 (08) :673-682

[3]

BREW K., 2003, ADV DAIRY CHEM, P387, DOI [10.1007/978-1-4419-8602-38, DOI 10.1007/978-1-4419-8602-38]

[4]

Byler D. M., 1989, C P 7 INT C FOUR TRA

[5] EXAMINATION OF THE SECONDARY STRUCTURE OF PROTEINS BY DECONVOLVED FTIR SPECTRA [J].

BYLER, DM ;

SUSI, H .

BIOPOLYMERS, 1986, 25 (03) :469-487

[6] Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate [J].

Chandrapala, Jayani ;

Zisu, Bogdan ;

Palmer, Martin ;

Kentish, Sandra ;

Ashokkumar, Muthupandian .

ULTRASONICS SONOCHEMISTRY, 2011, 18 (05) :951-957

[7]

CHERRY J P., 1981, Protein Functionality in Foods ACS Symposium Series 147, P149

[8]

Chobert J., 2012, J BIOSCI BIOTECHNOL, V1, P171

[9] Foaming and interfacial properties of hydrolyzed β-lactoglobulin [J].

Davis, JP ;

Doucet, D ;

Foegeding, EA .

JOURNAL OF COLLOID AND INTERFACE SCIENCE, 2005, 288 (02) :412-422

[10] FOOD COLLOIDS - AN OVERVIEW [J].

DICKINSON, E .

COLLOIDS AND SURFACES, 1989, 42 (1-2) :191-204

← 1 2 3 4 5 6 →