Effect of phosphatase/transglutaminase treatment on molar mass distribution and techno-functional properties of sodium caseinate

被引:16
作者
Hiller, Beate [1 ]
Lorenzen, Peter Chr [1 ]
机构
[1] Max Rubner Inst, Dept Safety & Qual Milk & Fish Prod, D-24103 Kiel, Germany
关键词
Sodium caseinate; Dephosphorylation; Transglutaminase; Techno-functional properties; ENZYMATIC CROSS-LINKING; BETA-CASEIN; MICROBIAL TRANSGLUTAMINASE; DEPHOSPHORYLATED CASEIN; EMULSIFYING PROPERTIES; BOVINE CASEIN; WHOLE CASEIN; PROTEINS; EPSILON-(GAMMA-GLUTAMYL)LYSINE; POLYMERIZATION;
D O I
10.1016/j.lwt.2008.06.003
中图分类号
TS2 [食品工业];
学科分类号
100403 [营养与食品卫生学];
摘要
Sodium caseinate was enzymatically dephosphorylated by alkaline or acid phosphatase prior to incubation with microbial transglutaminase. It was demonstrated that a higher degree of protein cross-linking by transglutaminase was achieved in dephosphorylated sodium caseinate than in non-dephosphorylated sodium caseinate. During transglutaminase treatment, about 70% protein polymers >200.000 g/mol were produced from untreated sodium caseinate, but about 90% protein polymers >200.000 g/mol from dephosphorylated sodium caseinate. Phosphatase/transglutaminase-treated sodium caseinate exhibited techno-functional properties similar to transglutaminase-treated sodium caseinate, but performed improved interfacial stabilisation behaviour as well as higher viscosity. (C) 2008 Swiss Society of Food Science and Technology. Published by Elsevier Ltd. All rights reserved.
引用
收藏
页码:87 / 92
页数:6
相关论文
共 40 条
[1]
Akuzawa Ryozo, 2004, Animal Science Journal, V75, P385, DOI 10.1111/j.1740-0929.2004.00202.x
[2]
PROPERTIES OF DEPHOSPHORYLATED ALPHAS1-CASEIN - PRECIPITATION BY CALCIUM-IONS AND MICELLE FORMATION [J].
BINGHAM, EW ;
CARROLL, RJ ;
FARRELL, HM .
BIOCHEMISTRY, 1972, 11 (13) :2450-&
[3]
Improvement of dough rheology, bread quality and bread shelf-life by enzymes combination [J].
Caballero, P. A. ;
Gomez, M. ;
Rosell, C. M. .
JOURNAL OF FOOD ENGINEERING, 2007, 81 (01) :42-53
[4]
Dependence of the interfacial behavior of β-casein on phosphoserine residues [J].
Cassiano, MM ;
Areas, JAG .
JOURNAL OF DAIRY SCIENCE, 2003, 86 (12) :3876-3880
[5]
Some properties of β-casein modified via phosphatase [J].
Darewicz, M ;
Dziuba, J ;
Minkiewicz, P .
ACTA ALIMENTARIA, 2005, 34 (04) :403-415
[6]
Dephosphorylation-induced structural changes in β-casein and its amphiphilic fragment in relation to emulsion properties [J].
Darewicz, M ;
Dziuba, J ;
Caessens, PWJR ;
Gruppen, H .
BIOCHIMIE, 2000, 82 (03) :191-195
[7]
Polymerization and gelation of whey protein isolates at low pH using transglutaminase enzyme [J].
Eissa, AS ;
Bisram, S ;
Khan, SA .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2004, 52 (14) :4456-4464
[8]
TISSUE SULFHYDRYL GROUPS [J].
ELLMAN, GL .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1959, 82 (01) :70-77
[9]
Effect of cross-linking with transglutaminase on the heat stability and some functional characteristics of sodium caseinate [J].
Flanagan, J ;
Gunning, Y ;
FitzGerald, RJ .
FOOD RESEARCH INTERNATIONAL, 2003, 36 (03) :267-274
[10]
Functional properties of Bacillus proteinase hydrolysates of sodium caseinate incubated with transglutaminase pre- and post-hydrolysis [J].
Flanagan, J ;
FitzGerald, RJ .
INTERNATIONAL DAIRY JOURNAL, 2003, 13 (2-3) :135-143