Modification of the structural and rheological properties of β-lactoglobulin/κ-carrageenan mixed gels induced by high pressure processing

被引:25
作者
Li, Xiaoying [1 ]
He, Xiaoye [1 ]
Mao, Like [1 ]
Gao, Yanxiang [1 ]
Yuan, Fang [1 ]
机构
[1] China Agr Univ, Coll Food Sci & Nutr Engn, Key Lab Funct Dairy, Minist Educ, Beijing 100083, Peoples R China
基金
中国国家自然科学基金; 国家重点研发计划;
关键词
beta-lactoglobulin; kappa-carrageenan; Mixed gels; High pressure processing; Gel properties; THERMAL GELLING PROPERTIES; KAPPA-CARRAGEENAN; PROTEIN GEL; POLYSACCHARIDES; HYDROGELS; GELATION; PH;
D O I
10.1016/j.jfoodeng.2019.109851
中图分类号
TQ [化学工业];
学科分类号
0817 ;
摘要
High pressure processing (HPP) is an emerging non-thermal processing technology and a preparation method to induce protein-polysaccharide mixed gels, which can encapsulate and delivery thermosensitive bioactive compounds. This study investigated the properties of p-lactoglobulin (beta-Lg)/kappa-carrageenan (kappa-car) mixed gels induced by HPP (0.1-600 MPa for 30 min, 25 degrees C) with different ratios of beta-Lg to kappa-car at pH 3.0, 5.0 and 7.0. The results showed that the pressure required to form beta-Lg/kappa-car mixed gels was at least 400 MPa when the beta-Lg/kappa-car mass ratio increased to 14:1 at all tested pH values. The water holding capacity and textural properties increased with the increase of pressure levels. The hydrophobic interaction was dominant in the mixed gels induced by HPP at all pH values, and the network structure was more compact and smoother with higher pressure.
引用
收藏
页数:10
相关论文
共 42 条
[1]  
[Anonymous], FOOD CHEM
[2]  
[Anonymous], MOD FOOD SCI TECHNOL
[3]  
Balasubramaniam VM, 2008, FOOD TECHNOL-CHICAGO, V62, P32
[4]   INTERACTIONS IN PROTEIN POLYSACCHARIDE CALCIUM GELS [J].
BERNAL, VM ;
SMAJDA, CH ;
SMITH, JL ;
STANLEY, DW .
JOURNAL OF FOOD SCIENCE, 1987, 52 (05) :1121-&
[5]   Structural changes of β-lactoglobulin during thermal unfolding and refolding -: An FT-IR and circular dichroism study [J].
Bhattacharjee, C ;
Saha, S ;
Biswas, A ;
Kundu, M ;
Ghosh, L ;
Das, KP .
PROTEIN JOURNAL, 2005, 24 (01) :27-35
[6]   The mechanism of high pressure-induced gels of rabbit myosin [J].
Cao, Yingying ;
Xia, Tianlan ;
Zhou, Guanghong ;
Xu, Xinglian .
INNOVATIVE FOOD SCIENCE & EMERGING TECHNOLOGIES, 2012, 16 :41-46
[7]   Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region [J].
Carbonaro, M. ;
Nucara, A. .
AMINO ACIDS, 2010, 38 (03) :679-690
[8]   Effects of high pressure level and holding time on properties of duck muscle gels containing 1% curdlan [J].
Chen, Conggui ;
Wang, Rui ;
Sun, Gaojun ;
Fang, Hongmei ;
Ma, Daorong ;
Yi, Shoulian .
INNOVATIVE FOOD SCIENCE & EMERGING TECHNOLOGIES, 2010, 11 (04) :538-542
[9]   Effects of high pressure processing on the thermal gelling properties of chicken breast myosin containing κ-carrageenan [J].
Chen, Xing ;
Chen, Cong-gui ;
Zhou, Yan-zi ;
Li, Pei-jun ;
Ma, Fei ;
Nishiumi, Tadayuki ;
Suzuki, Atsushi .
FOOD HYDROCOLLOIDS, 2014, 40 :262-272
[10]   Influence of high-pressure treatment on β-lactoglobulin-pectin associations in emulsions and gels [J].
Dickinson, E ;
James, JD .
FOOD HYDROCOLLOIDS, 2000, 14 (04) :365-376