ASPARTIC PROTEINASES IN WHEAT-FLOUR .2. ENRICHMENT

被引:3
作者
TIMMERMANN, F
BELITZ, HD
机构
[1] TECH UNIV MUNICH,DEUTSCH FORSCH ANSTALT LEBENSMITTELCHEM,INST LEBENSMITTELCHEM,W-8046 GARCHING,GERMANY
[2] KURT HESS INST MEHL & EIWEISSFORSCH,W-8046 GARCHING,GERMANY
来源
ZEITSCHRIFT FUR LEBENSMITTEL-UNTERSUCHUNG UND-FORSCHUNG | 1993年 / 196卷 / 01期
关键词
D O I
10.1007/BF01192977
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Proteinases in wheat flour, which are active against azocasein at pH 5.0 and inhibited by pepstatin, were enriched by precipitation with ammonium sulphate, affinity chromatography on haemoglobin Sepharose 4B and ion exchange chromatography on carboxymethylallulose. The crude enzyme preparation delivered eleven active fractions on carrier-free isoelectric focusing in the pH range 4.76-5.66. The two main peaks exhibited isoelectric points of 5.05 and 5.24 respectively, and were free of exoproteolytic activities. The amino acid compositions of the active fractions were similar and characterized by about 50 mol% of Glu, Gly and Ser.
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页码:12 / 16
页数:5
相关论文
共 12 条
[1]  
BEISENHERZ G, 1953, Z NATURFORSCH, V86, P555
[2]   PURIFICATION OF WHEAT PROTEASES BY AFFINITY CHROMATOGRAPHY ON HEMOGLOBIN-SEPHAROSE COLUMN [J].
CHUA, GK ;
BUSHUK, W .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1969, 37 (03) :545-&
[3]  
DOI E, 1980, AGR BIOL CHEM TOKYO, V44, P741, DOI 10.1080/00021369.1980.10864028
[4]  
GORG A, 1981, LKB320 APPL NOT
[5]  
KAMINSKI E, 1969, CEREAL CHEM, V46, P317
[6]  
MCDONALD CE, 1964, CEREAL CHEM, V41, P443
[7]  
Olcott H. S., 1943, CEREAL CHEM, V20, P87
[8]   PURIFICATION AND PROPERTIES OF 2 PROTEOLYTIC-ENZYMES WITH CARBOXYPEPTIDASE ACTIVITY IN GERMINATED WHEAT [J].
PRESTON, KR ;
KRUGER, JE .
PLANT PHYSIOLOGY, 1976, 58 (04) :516-520
[9]  
TIMMERMANN F, 1992, IN PRESS Z LEBENSM U
[10]  
TIMMERMANN F, 1984, THESIS TU MUNCHEN