Sequential ultrasound and transglutaminase treatments improve functional, rheological, and textural properties of whey protein concentrate

被引：57

作者：

Ahmadi, Zahra ^{[1
]}

Razavi, Seyed Mohammad Ali ^{[1
]}

Varidi, Mahdi ^{[1
]}

机构：

[1] Ferdowsi Univ Mashhad, Dept Food Sci & Technol, Food Hydrocolloids Res Ctr, POB 91775-1163, Mashhad, Iran

来源：

INNOVATIVE FOOD SCIENCE & EMERGING TECHNOLOGIES | 2017年 / 43卷

关键词：

Modification; Rheology; Texture; TGase; Ultrasound; Whey; HIGH-INTENSITY ULTRASOUND; CROSS-LINKING; MICROBIAL TRANSGLUTAMINASE; BETA-LACTOGLOBULIN; FOAMING PROPERTIES; ALPHA-LACTALBUMIN; MILK WHEY; PH; ISOLATE; CASEIN;

D O I：

10.1016/j.ifset.2017.08.013

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

In this study, the combined effect of ultrasound pretreatment (US) and microbial transglutaminase (MTG) on the rheological, textural, and functional attributes of whey protein concentrate (WPC) were investigated. All the samples exhibited non-Newtonian shear-thinning behavior. Treatment with US lead to a significant increase in foaming capacity, gel hardness, and adhesiveness at 7.5 min, while reduced emulsifying capacity and syneresis at all levels. Moreover, consistency coefficient, foam stability, emulsifying capacity, emulsion stability, gel hardness and adhesiveness improved, whereas a slight decrease was observed in foaming capacity and syneresis of gels as a consequence of TG treatment respectively. 5 min US - 5 U.g(-1) pr TG treated sample exhibited the least syneresis value of all samples. SEM images affirmed the beneficial effects of treatments on texture, reduction of voids size and supported the textural results. Overall, ongoing US pretreatment and TG treatment were successful in modifying the functional properties of whey proteins. Industrial relevance: Food industry is consuming whey proteins for their functional characteristics besides their nutritional value. Microbial transglutaminase (MTG) can modify whey protein structure. High intensity ultrasound (HIU) is also mentioned as a material-altering technology. Heat denaturation is used for changing whey protein structure before enzyme treatment. The purpose of this study was to investigate the feasibility of replacing heat denaturation by ultrasound treatment before transglutaminase addition to a whey protein system. We also aimed to test the simultaneous effect of US and TG in order to meet emerging demands and produce different novel targeted products. Our results indicated that US treatment may replace heat denaturation before TG treatment and combination of these two factors improved various properties of whey protein systems.

引用

页码：207 / 215

页数：9

共 39 条

[1] Emulsifying and foaming properties of transglutaminase-treated wheat gluten hydrolysate as influenced by pH, temperature and salt [J].

Agyare, Kingsley K. ;

Addo, Kwaku ;

Xiong, Youling L. .

FOOD HYDROCOLLOIDS, 2009, 23 (01) :72-81

[2] pH-Stability and Thermal Properties of Microbial Transglutaminase-Treated Whey Protein Isolate [J].

Agyare, Kingsley K. ;

Damodaran, Srinivasan .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2010, 58 (03) :1946-1953

[3] PURIFICATION AND CHARACTERISTICS OF A NOVEL TRANSGLUTAMINASE DERIVED FROM MICROORGANISMS [J].

ANDO, H ;

ADACHI, M ;

UMEDA, K ;

MATSUURA, A ;

NONAKA, M ;

UCHIO, R ;

TANAKA, H ;

MOTOKI, M .

AGRICULTURAL AND BIOLOGICAL CHEMISTRY, 1989, 53 (10) :2613-2617

[4] Altering functional attributes of proteins through cross linking by transglutaminase - A case study with whey and seed proteins [J].

Anuradha, S. N. ;

Prakash, V. .

FOOD RESEARCH INTERNATIONAL, 2009, 42 (09) :1259-1265

[5] Comparative study of high intensity ultrasound effects on food proteins functionality [J].

Arzeni, C. ;

Martinez, K. ;

Zema, P. ;

Arias, A. ;

Perez, O. E. ;

Pilosof, A. M. R. .

JOURNAL OF FOOD ENGINEERING, 2012, 108 (03) :463-472

[6] Functionality of β-casein peptides:: Importance of amphipathicity for emulsion-stabilizing properties [J].

Caessens, PWJR ;

Gruppen, H ;

Slangen, CJ ;

Visser, S ;

Voragen, AGJ .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1999, 47 (05) :1856-1862

[7] The effects of high-intensity ultrasound on the structural and functional properties of α-Lactalbumin, β-Lactoglobulin and their mixtures [J].

Chandrapala, Jayani ;

Zisu, Bogdan ;

Kentish, Sandra ;

Ashokkumar, Muthupandian .

FOOD RESEARCH INTERNATIONAL, 2012, 48 (02) :940-943

[8] Heat-induced redistribution of disulfide bonds in milk proteins.: 1.: Bovine β-lactoglobulin [J].

Creamer, LK ;

Bienvenue, A ;

Nilsson, H ;

Paulsson, M ;

van Wanroij, M ;

Lowe, EK ;

Anema, SG ;

Boland, MJ ;

Jiménez-Flores, R .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2004, 52 (25) :7660-7668

[9]

Damodaran S, 2005, J FOOD SCI, V70, pR54

[10]

Damodaran S., 2008, Fennema's food chemistry, V4th ed., DOI DOI 10.1201/9781420020526

← 1 2 3 4 →