Inhibitory effect of melanoidins from glucose-asparagine on carboxypeptidases activity

被引:14
作者
Ibarz, A. [1 ]
Garza, S. [1 ]
Pagan, J. [1 ]
机构
[1] Univ Lleida, Dept Tecnol Aliments UTPV, CeRTA, Lleida 25198, Spain
关键词
carboxypeptidase; melanoidin; enzyme inhibition; enzyme activity;
D O I
10.1007/s00217-007-0655-3
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
This paper shows the effect of melanodins obtained from a glucose/asparagine system and also the effect of excess of substrate on the activity of the carboxypeptidase A (CPA) and carboxypeptidase B (CPB) enzymes. It was found that the substrate might have an inhibiting effect at high concentration. The presence of melanoidins has an inhibitory effect on both enzymes, with the value of the maximum reaction rate of the enzymatic reaction decreasing with the increase in melanoidins, so that for CPA, a value of nil was obtained for the above-mentioned maximum reaction rate for melanoidin concentrations of 0.042% (w/v), while the maximum reaction rate value for CPB is nil for a concentration of 0.077% (w/v).
引用
收藏
页码:1277 / 1282
页数:6
相关论文
共 16 条
[1]   INFLUENCE OF STORAGE ON THE COMPOSITION OF CLARIFIED APPLE JUICE CONCENTRATE [J].
BABSKY, NE ;
TORIBIO, JL ;
LOZANO, JE .
JOURNAL OF FOOD SCIENCE, 1986, 51 (03) :564-567
[2]  
BERGMEYER HU, 1974, METHODS ENZYMATIC AN
[3]  
DIXON M, 1979, ENZYMES, P60
[4]  
Folk J.E., 1971, ENZYMES, V3, P57
[5]  
FOLK JE, 1960, J BIOL CHEM, V235, P2272
[6]   BLOCKAGE OF PROTEIN ENZYMATIC DIGESTION (CARBOXYPEPTIDASE-B) BY HEAT-INDUCED SUGAR-LYSINE REACTIONS [J].
HANSEN, LP ;
MILLINGTON, RJ .
JOURNAL OF FOOD SCIENCE, 1979, 44 (04) :1173-1177
[7]  
Hartsuck J. A., 1971, ENZYMES, V3, P1
[8]   Kinetic analysis of the inhibition by melanoidin of trypsin [J].
Hirano, M ;
Miura, M ;
Gomyo, T .
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 1996, 60 (03) :458-462
[9]   MELANOIDIN AS A NOVEL TRYPSIN-INHIBITOR [J].
HIRANO, M ;
MIURA, M ;
GOMYO, T .
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 1994, 58 (05) :940-941
[10]  
HUIJGHEBAERT SM, 1986, J LIPID RES, V27, P742