Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration

被引:217
作者
Wu, WU [1 ]
Hettiarachchy, NS [1 ]
Qi, M [1 ]
机构
[1] Univ Arkansas, Dept Food Sci, Fayetteville, AR 72704 USA
关键词
emulsifying properties; enzymatic modification; hydrophobicity; papain; solubility; soy protein isolate; ultrafiltration;
D O I
10.1007/s11746-998-0235-0
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Peptide size control is important for obtaining desirable functional properties so that these peptides can be better utilized. Proteolytic enzymatic modification of soy protein isolates (SPI), followed by ultrafiltration, is an effective way to fractionate these proteins into peptides with controlled molecular size. SPI was predenatured by mild alkali at pH 10 and heated at 50 degrees C for 1 h prior to partial hydrolysis by papain at pH 7.0 and 38 degrees C for 10, 30, and 60 min (PMSPI10, PMSPI30, and PMSPI60). The hydrolysate PMSPI60 was further fractionated by ultrafiltration wish a stirred cell and disc membranes (100-, 50-, and 20-kDa molecular weight cut-off) into one retentate (R100) and three permeates (P100, P50, and P20). Molecular weighs distribution, surface hydrophobicity (S-0), protein solubility (PS), emulsifying activity index (EAI), and emulsion stability index (ESI) of the control SPI (without added papain), hydrolysates, and ultrafiltrates were investigated. Significant increases (P < 0.001) in S-0, PS, EAI, and ESI were observed in the hydrolysates. Peptides in the permeates had higher PS and EAI but lower So than the peptides in the retentate and hydrolysate. Soy protein peptides that were prepared from SPI by papain modification and ultrafiltration had lower molecular weight, higher solubility, and higher emulsifying properties. They could find use in products that require these properties, especially in the cosmetic and health food industries.
引用
收藏
页码:845 / 850
页数:6
相关论文
共 25 条
[1]   DETERMINATION OF THE DEGREE OF HYDROLYSIS OF FOOD PROTEIN HYDROLYSATES BY TRINITROBENZENESULFONIC ACID [J].
ADLERNISSEN, J .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1979, 27 (06) :1256-1262
[2]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[3]  
CHERYAN M, 1993, ADV FOOD ENG, P165
[4]  
CHERYAN M, 1986, ULTRAFILTRATION HDB
[5]   SOLUBILITY AND EMULSIFYING PROPERTIES OF CASEINS AND WHEY PROTEINS MODIFIED ENZYMATICALLY BY TRYPSIN [J].
CHOBERT, JM ;
BERTRANDHARB, C ;
NICOLAS, MG .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1988, 36 (05) :883-892
[6]   FUNCTIONAL-PROPERTIES OF SOY PROTEIN HYDROLYSATES FROM A CONTINUOUS ULTRAFILTRATION REACTOR [J].
DEESLIE, WD ;
CHERYAN, M .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1988, 36 (01) :26-31
[7]   FRACTIONATION OF SOY PROTEIN HYDROLYSATES USING ULTRAFILTRATION MEMBRANES [J].
DEESLIE, WD ;
CHERYAN, M .
JOURNAL OF FOOD SCIENCE, 1992, 57 (02) :411-413
[8]  
DEESLIE WD, 1981, J FOOD SCI, V46, P1035, DOI 10.1111/j.1365-2621.1981.tb02987.x
[9]   RELATIONSHIPS OF HYDROPHOBICITY AND NET CHARGE TO THE SOLUBILITY OF MILK AND SOY PROTEINS [J].
HAYAKAWA, S ;
NAKAI, S .
JOURNAL OF FOOD SCIENCE, 1985, 50 (02) :486-491
[10]   RELATIONSHIP BETWEEN SURFACE FUNCTIONAL-PROPERTIES AND FLEXIBILITY OF PROTEINS DETECTED BY THE PROTEASE SUSCEPTIBILITY [J].
KATO, A ;
KOMATSU, K ;
FUJIMOTO, K ;
KOBAYASHI, K .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1985, 33 (05) :931-934