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Plant Physiology 1986-Dec

Stem infusions enhanced methionine content of soybean storage protein.

Vetëm përdoruesit e regjistruar mund të përkthejnë artikuj
Identifikohuni Regjistrohu
Lidhja ruhet në kujtesën e fragmenteve
L J Grabau
D G Blevins
H C Minor

Fjalë kyçe

Abstrakt

The quality of soybean (Glycine max [L.] Merrill) seed storage protein is limited by its low methionine (Met) content. Met supplementation of an in vitro soybean cotyledon culture has been shown to increase Met content by 21.9% due to an inhibition of the synthesis of the Met-devoid beta subunit of 7S storage protein (JF Thompson et al. 1981, Phytochemistry 20: 941-945). The objective of this research was to determine if Met supplementation of intact plants would result in a similar improvement in soybean protein quality. A solution including 10 millimolar d,l malic acid plus 10 millimolar K(2)HPO(4) with or without 20 millimolar d,l Met or 20 millimolar Na(2)SO(4) was infused throughout seed development into lower stem internodes of soybeans (cv ;Williams 79' or ;Williams 82') grown under both greenhouse and field conditions. Pediatric intravenous kits were used to infuse an average of 51.2 milliliters per plant. Met content of whole soybean seeds from intact plants receiving Met infusions increased by as much as 22.7%. Even greater (up to 31.0%) increases in cysteine (Cys) content were noted, indicating that soybean plants are able to metabolize Met to Cys, or that supplemental Met allows Cys accumulation by some other mechanism. Electrophoretic patterns showed a dramatic decrease in the synthesis of the beta subunit of 7S storage protein when Met was supplemented, and this effect was not confined to seeds at the lower nodes. In addition, seeds from upper compared to lower plant nodes (regardless of infusion treatment) had greater protein content (45.0 versus 41.6 w/w%), and different protein composition, as indicated by significantly different amino acid profiles. Methionine supplementation of intact soybean plants improved protein quality through an alteration in storage protein composition.

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