Peptide characteristics of sunflower protein hydrolysates

被引:66
作者
Villanueva, A
Vioque, J
Sánchez-Vioque, R
Clemente, A
Pedroche, J
Bautista, J
Millán, F
机构
[1] Inst Grasa, Seville 41012, Spain
[2] Univ Sevilla, Fac Farm, Dept Bioquim Bromatol & Toxicol, E-41012 Seville, Spain
关键词
alcalase; enzymatic hydrolysis; flavourzyme; sunflower proteins;
D O I
10.1007/s11746-999-0184-2
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Protein isolate from sunflower seeds was used as the starting material for preparation of an extensively hydrolyzed peptide product. Protein was hydrolyzed using an endopeptidase (Alcalase), an exopeptidase (Flavourzyme), or both enzymes sequentially. Combined use of these proteases generated the highest degree of hydrolysis, 54.2%, and highest solubility, around 90%, between pH 2.5 and 7. Molecular weight profiles of the hydrolysates were characterized by gel filtration chromatography and denaturing electrophoresis. Amino acid compositions and solubilities of the different hydrolysates also were studied. Paper no. J9208 in JAOCS 76, 1455-1460 (December 1999).
引用
收藏
页码:1455 / 1460
页数:6
相关论文
共 20 条
[1]  
Adler-Nissen J., 1986, ENZYMATIC HYDROLYSIS, P263
[2]   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
[3]   AMINO-ACID-ANALYSIS BY HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY AFTER DERIVATIZATION WITH DIETHYL ETHOXYMETHYLENEMALONATE [J].
ALAIZ, M ;
NAVARRO, JL ;
GIRON, J ;
VIOQUE, E .
JOURNAL OF CHROMATOGRAPHY, 1992, 591 (1-2) :181-186
[4]  
AOAC, 1990, AOAC OFFICIAL METHOD, P1
[5]  
Chobert JM, 1996, NAHRUNG, V40, P177, DOI 10.1002/food.19960400403
[6]   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
[7]  
FAO/WHO, 1991, PROT QUAL EV, P66
[8]  
HESSOV I, 1983, ACTA CHIR SCAN, V516, P26
[9]   CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4 [J].
LAEMMLI, UK .
NATURE, 1970, 227 (5259) :680-+
[10]   ACTION OF TRANSGLUTAMINASE ON THE CONSTITUTIVE POLYPEPTIDES OF PEA LEGUMIN [J].
LARRE, C ;
CHIARELLO, M ;
DUDEK, S ;
CHENU, M ;
GUEGUEN, J .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1993, 41 (11) :1816-1820