323 research outputs found
Nutritional composition and consumer acceptability study of different preparations of edamame soy beans.
Masters Degree. University of KwaZulu-Natal, Pietermaritzburg.The aim of this study was to determine the nutritional composition and physical properties of dry mature and roasted mature Edamame beans and to compare, through sensory evaluation, the consumer accessibility of these products in grade 5 learners. Soy beans have been known and recognised for centuries as a plant food that, when compared with other plants, is high in protein. For this reason, soy beans have historically been called ‘meat of the field’. The overall energy content of the Edamame soy beans remained unchanged after undergoing oven and microwave roasting. Even though the microwave roasted soy bean samples appeared to have a higher macronutrient content when compared to oven roasted soy bean samples, it is important to recognize the fact that microwave roasting causes more water loss, which has a concentrating effect on the macronutrients. Forty-one grade 5 learners participated in a sensory evaluation, conducted at Cato Crest Primary School in Durban, KwaZulu-Natal. In this study, learners preferred the Edamame above their usual sweet-flavoured snacks. The learners however, preferred samples that had strong "sweet" and monosodium glutamate flavours. Results from this study suggest that the different roasting methods of Edamame beans do not yield products that are significantly different in terms of nutritional quality. Yet, microwave roasting caused more fluid loss. This makes microwave roasting ideal to process Edamame soy beans due to improved shelf life. Edamame soy beans are a healthier source of protein in comparison to peanuts as it provides good quality protein with a lower fat content. It provides all of the essential amino acids for adults and children and would be a good alternative source of protein if made more available to those at risk of malnutrition
Theory of ultrafast quasiparticle dynamics in high-temperature superconductors: Pump fluence dependence
We present a theory for the time-resolved optical spectroscopy of
high-temperature superconductors at high excitation densities with strongly
anisotropic electron-phonon coupling. A signature of the strong coupling
between the out-of-plane, out-of-phase O buckling mode () and
electronic states near the antinode is observed as a higher-energy peak in the
time-resolved optical conductivity and Raman spectra, while no evidence of the
strong coupling between the in-plane Cu-O breathing mode and nodal electronic
states is observed. More interestingly, it is observed that under appropriate
conditions of pump fluence, this signature exhibits a re-entrant behavior with
time delay, following the fate of the superconducting condensate.Comment: 5 pages, 3 embedded eps figures, to appear in PR
Photoexcited electron dynamics in Kondo insulators and heavy fermions
We have studied the photoexcited carrier relaxation dynamics in the Kondo
insulator SmB6 and the heavy fermion metal YbAgCu4 as a function of temperature
and excitation level. The dynamic response is found to be both strongly
temperature dependent and nonlinear. The data are analyzed with a
Rothwarf-Taylor bottleneck model, where the dynamics are governed by the
presence of a narrow gap in the density of states near the Fermi level. The
remarkable agreement with the model suggests that carrier relaxation in a broad
class of heavy electron systems (both metals and insulators) is governed by the
presence of a (weakly temperature dependent) hybridization gap.Comment: accepted for publication in Physical Review Letter
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Regulation of an S6/H4 Kinase in Crude Lymphosarcoma P1798 Preparations
Purified S6/H4 kinase (Mr 60,000) requires autophosphorylation for activation. A rabbit anti-S6/H4 kinase peptide (SVIDPVPAPVGDSHVDGAAK) antibody recognized both the S6/H4 kinase holoenzyme and catalytic domain. Immunoreactivity with p60 kinase protein, and S6/H4 kinase activity were precisely correlated in fractions obtained from ion exchange chromatography of P1798 lymphosarcoma extracts. An enzyme which catalyzed the MgATP-dependent phosphorylation and activation of S6/H4 kinase coeluted with immunoreactivity from Mono 5, but not Mono Q chromatography. Since S6/H4 kinase is homologous with rac-activated PAK65, the observation that phosphorylation is also required for activation suggests a complex mechanism for in vivo activation of the S6/H4 kinase
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