Properties of gels induced by heat, protease, calcium salt, and acidulant from calcium ion-aggregated whey protein isolate

被引:22
作者
Ju, ZY [1 ]
Kilara, A [1 ]
机构
[1] Penn State Univ, Dept Food Sci, University Pk, PA 16802 USA
关键词
aggregation of whey proteins; gelation; microstructure; calcium;
D O I
10.3168/jds.S0022-0302(98)75684-X
中图分类号
S8 [畜牧、 动物医学、狩猎、蚕、蜂];
学科分类号
0905 ;
摘要
Gelation that was induced by heat, protease, calcium salt, or acidulant from a solution of Ca(2+) aggregated whey protein was investigated by analyses of the rheological, textural, and microstructural properties of the gel. The addition of 40 mM CaCl(2) to 18% whey protein solution resulted in aggregation during 4 h of incubation at 45 degrees C. The occurrence of aggregation was determined as increases in turbidity and in mean aggregate size. Hydrolysis by a protease from Bacillus licheniformis (1% enzyme to protein, wt/wt), a decline in pH by glucono-delta-lactone (1.5%, wt/vol), an increase in ionic strength with CaCl(2) (60 mM), or heat treatment (80 degrees C for 30 min) all led to gelation of the aggregated whey protein solutions within 40 min. The gels formed differed widely in texture and rheological properties. The heat-induced gel was over 20 times stronger than the gels that were induced by protease from Bacillus licheniformis, glucono-delta-lactone, and CaCl(2). The heat-induced gel also showed significantly highest adhesiveness. The gels induced by CaCl(2) and glucono-delta-lactone had significantly higher cohesiveness than the gels induced by heat or enzyme. The micrograph of the aggregated whey protein solution showed loose, irregular aggregates, which were reflected in gels induced by CaCl(2) or glucono-delta-lactone. The aggregates in the gels that were induced by heat or enzyme were larger than the parent aggregates. This difference may be due to fusion or to further aggregation of the parent aggregates during the inducement of gelation.
引用
收藏
页码:1236 / 1243
页数:8
相关论文
共 25 条
[1]   CA2+-INDUCED GELATION OF PRE-HEATED WHEY-PROTEIN ISOLATE [J].
BARBUT, S ;
FOEGEDING, EA .
JOURNAL OF FOOD SCIENCE, 1993, 58 (04) :867-871
[2]  
BOURNE MC, 1978, FOOD TECHNOL-CHICAGO, V32, P62
[3]  
DALGLEISH DG, 1986, DEV DAIRY CHEM, V1, P158
[4]   SPECIFIC DIVALENT CATION-INDUCED CHANGES DURING GELATION OF BETA-LACTOGLOBULIN [J].
FOEGEDING, EA ;
KUHN, PR ;
HARDIN, CC .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1992, 40 (11) :2092-2097
[5]  
FOEGEDING EA, 1992, IFT BAS SYM, V7, P423
[6]   Micellar transition state in casein between pH 5.5 and 5.0 [J].
Gastaldi, E ;
Lagaude, A ;
DelAFuente, BT .
JOURNAL OF FOOD SCIENCE, 1996, 61 (01) :59-+
[7]   ELECTRON-MICROSCOPIC STUDIES OF CASEIN MICELLES AND CURD MICROSTRUCTURE IN COTTAGE CHEESE [J].
GLASER, J ;
CARROAD, PA ;
DUNKLEY, WL .
JOURNAL OF DAIRY SCIENCE, 1980, 63 (01) :37-48
[8]   INTERMICELLAR RELATIONSHIPS IN RENNET-TREATED SEPARATED MILK .1. PREPARATION OF REPRESENTATIVE ELECTRON-MICROGRAPHS [J].
GREEN, ML ;
HOBBS, DG ;
MORANT, SV .
JOURNAL OF DAIRY RESEARCH, 1978, 45 (03) :405-+
[9]   Enzyme-induced gelation of whey proteins: Effect of protein denaturation [J].
Ju, ZY ;
Otte, J ;
Zakora, M ;
Qvist, KB .
INTERNATIONAL DAIRY JOURNAL, 1997, 7 (01) :71-78
[10]   PREPARATION AND PROPERTIES OF ACID-INDUCED GEL OF WHEY-PROTEIN [J].
KAWAMURA, F ;
MAYUZUMI, A ;
NAKAMURA, M ;
KOIZUMI, S ;
KIMURA, T ;
NISHIYA, T .
JOURNAL OF THE JAPANESE SOCIETY FOR FOOD SCIENCE AND TECHNOLOGY-NIPPON SHOKUHIN KAGAKU KOGAKU KAISHI, 1993, 40 (11) :776-782