scholarly journals Daily Periodicity of Attraction for Males to Females and Mating in the Sorghum Plant Bug, Stenotus rubrovittatus (Matsumura)

2009 ◽  
Vol 53 (2) ◽  
pp. 57-59 ◽  
Author(s):  
Toshinori Kichishima ◽  
Maki Fukuyama ◽  
Hiroya Higuchi ◽  
Akihiko Takahashi ◽  
Atsuhiko Nagasawa
BioResources ◽  
2020 ◽  
Vol 15 (4) ◽  
pp. 7933-7953
Author(s):  
Ryan J. Stoklosa ◽  
Renee J. Latona ◽  
Michael J. Powell ◽  
Madhav P. Yadav

Recovered hemicellulose fractions from biorefineries have the potential to improve overall process economics during the production of biofuels or other high value chemicals. A common hemicellulose found in many agricultural feedstocks is arabinoxylan (AX). This work investigated the influence of ferulic and p-coumaric acids on the antioxidant capability of AX hemicellulose recovered from sorghum bran, biomass, and bagasse. Sorghum bagasse and sorghum biomass AX contained the largest quantities of bound ferulic and p-coumaric acids at 13.1 mg/100 g and 6.3 mg/100 g, respectively. Antioxidant performance showed that sorghum bagasse AX hemicellulose produced the best reducing capability, while sorghum biomass and sorghum bran AX hemicellulose performed better as free radical scavengers. A reduction in free radical scavenging, as determined by the 1,1-diphenyl-2-picrylhydrazyl (DPPH) assay, occurred for sorghum bagasse and sorghum biomass AX hemicellulose at higher polysaccharide concentrations, which was either caused by the solution properties of the AX hemicelluloses or DPPH reaction reversibility in the presence of phenolic compounds with methoxy content. Alternatively, H2O2 scavenging by the AX hemicellulose revealed a dose-dependent response. Although scavenging effect was reduced at higher concentrations, sorghum bagasse AX hemicellulose functioned as having the best antioxidant capacity with respect to total reducing capability.


1986 ◽  
Vol 41 (1-2) ◽  
pp. 79-86 ◽  
Author(s):  
Daniel L. Siehl ◽  
James A. Connelly ◽  
Eric E. Conn

Abstract A stable activity which transfers the amino group from glutamate to prephenate was extracted from 4-day old etiolated shoots of sorghum. The activity was retained on DEAE cellulose and eluted as a single peak. Prephenate aminotransferase co-eluted with a very abundant α-ketoglutarate: aspartate aminotransferase, but heating at 70 °C resulted in loss of α-ketoglutarate: aspar­tate activity with nearly full retention of prephenate: glutamate aminotransferase activity. The heated enzyme displayed high affinity and specificity for prephenate. Among 7 donors tested, only glutamate, and aspartate at less than 20% the rate with glutamate, supported prephenate aminotransferase activity. In the reverse direction, a reaction rate comparable to that in the forward direction was unchanged as the concentration of α-ketoglutarate was reduced from 1.0 to 0.09 mᴍ. The apparent Km for arogenate was 0.8 mᴍ. The forward reaction was unaffected by the inclusion of tyrosine, phenylalanine or tryptophan. Together with the discovery of arogenate dehydrogenase in sorghum [3], these data indicate that, in the sorghum plant, tyrosine derives from prephenate by transamination and aromatization. rather than the reverse sequence.


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