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Wheat Information
Service
Number 76: 80-82
(1993)
Relation
between wheat seed storage protein subunits and noodle
viscoelasticity
H. Nakamura and H. Yoshida
National Agriculture Research Center Kannondai, Tsukuba, Ibaraki
305, Japan
Summary
A comparison was made of the electrophoretic patterns of Wheat
seed storage proteins for Kanto 107, a wheat (Triticum
aestivum L.) line with good noodle viscoelasticity, and Norin 61,
a wheat cultivar with standard viscoelasticity. A protein band with
molecular weight of 53 kD was detected in Kanto 107, but not in Norin
61. A band with molecular weight of 129 kD was found in Norin
61, but not in Kanto 107. When Kanto 107 was cultivated in winter
cropping on drained paddy fields, viscoelasticity was found to
decrease, the 53 kD subunit disappeared from the electrophoretic
pattern and the 129 kD subunit appeared. These subunits thus appear
to relate to viscoelasticity.
Introduction
Wheat (Triticum aestivum L.) seed storage protein consists
of glutenin, gliadin, globulin and albumin. Glutenin and gliadin
account for about 80% total seed storage protein content, and this
feature is closely related to bread making quality (Payne et al
1984), flour hardness (Nakamura et al 1990) and Chinese noodle making
quality (Huang et al 1988). Japanese noodle making quality may also
possibly be associated with seed protein composition. In this study,
a comparison was made of electrophoretic patterns between a wheat
line and a cultivar differing in noodle making quality, so as to
determine the relation between seed storage protein subunits and
noodle viscoelasticity.
Materials and methods
Kanto 107, a wheat line with good noodle viscoelasticity and
Norin 61, a cultivar with standard viscoelasticity were used, Four
Kankei lines obtained by crossing with Kanto 107 as a maternal parent
were also used. The materials were cultivated three times in 1988 to
1991 in an upland and a paddy field double-cropped with rice. Flour
(5 mg) was suspended in the sample buffer (2% sodium dodecyl sulfate
(SDS), 10% glycerol, 5% 2-mercaptoetanol and 0.0625 M Tris-HCL pH
6.8) and shaken for 2 hr. The sully was heated at 95 oC
for 3 min and centrifuged at 15,000 xg for 3 min. The supernatant was
subjected to SDS-poly acrylamide gel electrophoresis (PAGE). Noodles
(10 g) were boiled in water for 20 min. Noodle viscoelasticity was
estimated by the sensory test of the Ministry of Agriculture,
Forestry and Fishries noodle quality test manual. Protein content was
analyzed by the Kjeldahl method.
Results and discussion
Fig.1
shows SDS-PAGE patterns of seed storage proteins from Norin 61 (lane
1-4) and Kanto 107 (lane 5-8). A subunit with molecular weight of 53
kD was detected in Kanto 107 cultivated in an upland field, but not
in Norin 61 cultivated in upland and paddy fields. In contrast, a
subunit with molecular weight of 129 kD was found in Norin 61 in
upland and paddy fields, but not in upland Kanto 107. Kanto 107 in
the upland field produced noodles with good viscoelasticity while
Norin 61 of low viscoelasticity was produced. According to the
experiments conducted in 1989-1990, when Kanto 107 was cultivated in
a paddy field, the 53 kD subunit disappeared and the 129 kD subunit
appeared. These viscoelasticity appeared to decrease. However, in the
experiment in 1991, protein subunits and viscoelasticity of Kanto 107
cultivated in the paddy field were identical to those of Kanto 107 in
the upland field. The protein content in 1991 was slightly higher
than that in 1989 and 1990, but the relationship between quantity and
quality of protein is not yet clear. Furthermore, investigation was
made in wheat Kankei lines. When the 53 kD subunit was present, but
not the 129 kD subunit, viscoelasticity was relatively high.
The 53 kD and 129 kD subunits thus appear to relate with noodle
viscoelasticity, though a definite conclusion requires further
research.
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