Improving the gel properties of transgenic microbial transglutaminase cross-linked soybean-whey mixed protein by ultrasonic pretreatment

被引：67

作者：

Cui, Qiang ^{[1
]}

Wang, Guorong ^{[2
]}

Gao, Da ^{[1
]}

Wang, Lin ^{[1
]}

Zhang, Anqi ^{[1
]}

Wang, Xibo ^{[1
]}

Xu, Ning ^{[1
]}

Jiang, Lianzhou ^{[1
]}

机构：

[1] Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China

[2] Leprino Foods Co, Denver, CO 80211 USA

来源：

PROCESS BIOCHEMISTRY | 2020年 / 91卷

关键词：

Microbial transglutaminase; Ultrasound; Gelation; Mixed proteins; HIGH-INTENSITY ULTRASOUND; BOVINE SERUM-ALBUMIN; IN-WATER EMULSIONS; SOY PROTEIN; EMULSIFYING PROPERTIES; INDUCED GELATION; PHYSICOCHEMICAL PROPERTIES; INDUCED AGGREGATION; FOOD PROTEINS; ISOLATE;

D O I：

10.1016/j.procbio.2019.12.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

This study investigated the effect of microbial transglutaminase cross-linking on the gel properties of soybean-whey mixed protein (SPI-WPI) after ultrasonic pretreatment. The average particle size of SPI-WPI decreased with increasing of ultrasonic time treatment, and minimal particle size was verified after 45 min. Endogenous fluorescence spectroscopy and surface hydrophobicity analysis showed that the SPI-WPI conformation changed after ultrasonic treatment. The polypeptide chain partially expanded inside the protein molecule, the hydrophobic group was exposed, and the protein structure became more stretched. The gel hardness and water holding capacity of the SPI-WPI hybrid system reached a maximum 30 min after ultrasonic treatment. Fourier infrared analysis showed that the secondary structure of the protein changed after ultrasonic modification. A complex is formed between SPI and WPI, and the gel properties of the mixed protein are significantly improved, providing theoretical and technical support for the development of new mixed protein foods.

引用

页码：104 / 112

页数：9

共 46 条

[1]

Abdullah M., 2003, Pakistan Journal of Nutrition, V2, P305

[2] Mixing animal and plant proteins: Is this a way to improve protein techno-functionalities? [J].

Alves, Alane Cangani ;

Tavares, Guilherme M. .

FOOD HYDROCOLLOIDS, 2019, 97

[3] 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

[4] Functionality of egg white proteins as affected by high intensity ultrasound [J].

Arzeni, Carolina ;

Perez, Oscar E. ;

Pilosof, Ana M. R. .

FOOD HYDROCOLLOIDS, 2012, 29 (02) :308-316

[5] Effect of solvent and temperature on the size distribution of casein micelles measured by dynamic light scattering [J].

Beliciu, C. M. ;

Moraru, C. I. .

JOURNAL OF DAIRY SCIENCE, 2009, 92 (05) :1829-1839

[6] Physico-chemical changes in heat treated micellar casein - Soy protein mixtures [J].

Beliciu, Cosmin M. ;

Moraru, Carmen I. .

LWT-FOOD SCIENCE AND TECHNOLOGY, 2013, 54 (02) :469-476

[7]

Cai M., 2012, 2012 13 INT THERM ME

[8] CONFORMATIONAL-CHANGES OF BOVINE SERUM-ALBUMIN UPON ITS ADSORPTION IN DODECANE-IN-WATER EMULSIONS AS REVEALED BY FRONT-FACE STEADY-STATE FLUORESCENCE [J].

CASTELAIN, C ;

GENOT, C .

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1994, 1199 (01) :59-64

[9] Effects of Ultrasound Pretreatment on the Enzymatic Hydrolysis of Soy Protein Isolates and on the Emulsifying Properties of Hydrolysates [J].

Chen, Lin ;

Chen, Jianshe ;

Ren, Jiaoyan ;

Zhao, Mouming .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2011, 59 (06) :2600-2609

[10] FLUORESCENCE AND STRUCTURE OF PROTEINS .8. IODINATION OF RIBONUCLEASE MODIFIED BY SUBTILISIN [J].

COWGILL, RW .

BIOCHIMICA ET BIOPHYSICA ACTA, 1966, 120 (02) :189-&

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