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COMPARATIVE STUDY OF CHEMICAL COMPOSITION AND PHYSICOCHEMICAL PROPERTIES OF DEFATTED WHEAT GERM FLOUR AND ITS PROTEIN ISOLATE
Author(s) -
ZHU KEXUE,
ZHOU HUIMING,
QIAN HAIFENG
Publication year - 2006
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2006.00067.x
Subject(s) - chemistry , potassium , food science , sodium , magnesium , cystine , extraction (chemistry) , rutin , polyacrylamide gel electrophoresis , composition (language) , tannic acid , gluten , zinc , biochemistry , chromatography , antioxidant , enzyme , cysteine , organic chemistry , linguistics , philosophy
Chemical composition and physicochemical properties of defatted wheat germ (WG) flour (DWGF) and protein isolate (DWGPI) were evaluated to determine their potential as food ingredients. Protein content of DWGF was 31.42% while that of DWGPI was 84.18%. Comparison of the amino acid composition to the Food and Agriculture Organization/World Health Organization reference pattern indicated that DWGF and DWGPI had well‐balanced amino acid profiles. Both of them were relatively rich in lysine, whereas cystine was lacking. The main mineral constituents of DWGF were potassium, magnesium and calcium, while sodium was the dominating element in DWGPI as a result of salt extraction. Concentrations of potassium, magnesium, calcium, manganese and zinc in DWGPI were significantly decreased because of alkaline extraction compared to those in DWGF. The elements copper and iron were higher in DWGPI than in DWGF. Total flavonoid content of DWGF was about 0.35 g rutin equiv/100 g, whereas that of DWGPI was lower (about 0.24 g rutin equiv/100 g). Compared to soybean protein isolate, DWGPI was easily digested by pepsin in vitro , while DWGF was comparatively indigestible. Nonreduced and reduced sodium dodecyl sulfate‐polyacrylamide gel electrophoresis analyses seem to show that interpolypeptide S‐S bonds were absent in the structure of WG proteins. DWGF and DWGPI shared four groups of bands: (1) 85–70 kDa; (2) 55–50 kDa; (3) 47–40 kDa; and (4) below 20 kDa.