Oligomerization of β-lactoglobulin by microbial transglutaminase during high pressure treatment

被引:22
作者
Lauber, S
Noack, I
Klostermeyer, H
Henle, T [1 ]
机构
[1] Tech Univ Dresden, Inst Lebensmittelchem, D-01062 Dresden, Germany
[2] Tech Univ Munich, Lehrstuhl Chem Biopolymere, D-85350 Freising Weihenstephan, Germany
关键词
transglutaminase; beta-lactoglobulin; high pressure; globular proteins; crosslinking;
D O I
10.1007/s002170100368
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
High pressure treatment of solutions of P-lactoglobulin in the presence of microbial transglutaminase for 60 min at 40 degreesC resulted in an enzyme-induced oligomerization of the whey protein at pressures of 400 MPa and to a less extent at 600 MPa. The degree of crosslinking was lower when transglutaminase was added to solutions of P-lactoglobulin after high pressure treatment and no oligomerization was detectable when the protein was incubated with transglutaminase under atmospheric pressure. Thus, microbial transglutaminase in combination with high pressure treatment offers new perspectives for the modification of globular proteins, which usually are not affected by the enzyme under atmospheric conditions.
引用
收藏
页码:246 / 247
页数:2
相关论文
共 18 条
[1]   CROSS-LINKING OF WHEY-PROTEIN BY TRANSGLUTAMINASE [J].
ABOUMAHMOUD, R ;
SAVELLO, P .
JOURNAL OF DAIRY SCIENCE, 1990, 73 (02) :256-263
[2]   Polymerization of beta-lactoglobulin and bovine serum albumin at oil-water interfaces in emulsions by transglutaminase [J].
Chanyongvorakul, Y ;
Matsumura, Y ;
Sawa, A ;
Nio, N ;
Mori, T .
FOOD HYDROCOLLOIDS, 1997, 11 (04) :449-455
[3]   TRANSGLUTAMINASE CATALYZES THE MODIFICATION OF GLUTAMINE SIDE-CHAINS IN THE C-TERMINAL REGION OF BOVINE BETA-LACTOGLOBULIN [J].
COUSSONS, PJ ;
PRICE, NC ;
KELLY, SM ;
SMITH, B ;
SAWYER, L .
BIOCHEMICAL JOURNAL, 1992, 283 :803-806
[4]   HIGH-PRESSURE UNFOLDING AND AGGREGATION OF BETA-LACTOGLOBULIN AND THE BAROPROTECTIVE EFFECTS OF SUCROSE [J].
DUMAY, EM ;
KALICHEVSKY, MT ;
CHEFTEL, JC .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1994, 42 (09) :1861-1868
[5]   Enzymatic cross-linking of whey proteins by a Ca2+-independent microbial transglutaminase from Streptomyces lydicus [J].
Faergemand, M ;
Otte, J ;
Qvist, KB .
FOOD HYDROCOLLOIDS, 1997, 11 (01) :19-25
[6]   Cross-linking of milk proteins with transglutaminase at the oil-water interface [J].
Faergemand, M ;
Murray, BS ;
Dickinson, E .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1997, 45 (07) :2514-2519
[7]   On the importance of using a Ca2+ independent transglutaminase for cross-linking of β-lactoglobulin [J].
Færgemand, M ;
Qvist, KB .
FOOD HYDROCOLLOIDS, 1999, 13 (03) :199-201
[8]  
Færgemand M, 1998, J AGR FOOD CHEM, V46, P884, DOI 10.1021/jf970733b
[9]  
Færgemand M, 1999, MILCHWISSENSCHAFT, V54, P563
[10]   Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase [J].
Han, XQ ;
Damodaran, S .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1996, 44 (05) :1211-1217