Impact of Rice Flour Cold-Water-Soluble Fraction Removal on Gelatinization and Pasting Properties

2014 ◽  
Vol 91 (5) ◽  
pp. 473-481 ◽  
Author(s):  
Guiai Jiao ◽  
Xiangjin Wei ◽  
Gaoneng Shao ◽  
Lihong Xie ◽  
Zhonghua Sheng ◽  
...  
1977 ◽  
Vol 1977 (1) ◽  
pp. 575-578 ◽  
Author(s):  
C. C. Brodersen ◽  
S. D. Rice ◽  
J. W. Short ◽  
T. A. Mecklenburg ◽  
J. F. Karinen

ABSTRACT The sensitivity of adult and larval Alaskan shrimp and crabs to the water-soluble fraction (WSF) of Cook Inlet crude oil was measured by tests using 96-hour static bioassays at the water termperatures that these animals normally encounter. Larval crustaceans were found to die more slowly than adults, making it necessary to measure sensitivity in terms of concentrations causing moribundity (death imminent) instead of in terms of concentrations causing death during exposure. The cessation of all motion and reaction was found to indicate moribundity in adults, and the cessation of swimming was found to indicate morbundity in larvae exposed for 96 hr. Ninety-six-hour LC50's for moribundity for stage I larvae ranged from 0.95 to 1.8 ppm depending on species, while 96-hr LC50's for adults ranged from 1.9 to 4.2 ppm oil. Sensitivities for stage I-VI larvae of coonstripe shrimp ranged between 0.24 ppm and 1.9 ppm. Larvae were more sensitive to oil than adults. The sensitivity of larvae depended on species and developmental stage. Larvae are probably more vulnerable than adults to oil exposure because of greater sensitivity to oil and greater susceptibility to predation. Cold-water species may be particularly vulnerable because of increased time spent as developing larvae.


1957 ◽  
Vol 35 (4) ◽  
pp. 241-250 ◽  
Author(s):  
W. G. Martin ◽  
J. E. Vandegaer ◽  
W. H. Cook

Livetin, the major water-soluble protein of hen egg yolk, was found to contain three major components having mobilities of −6.3, −3.8, and −2.1 cm.2 sec.−1 volt−1 at pH 8, µ 0.1, and these have been designated α-, β-, and γ-livetin respectively. The α- and β-livetins were separated and purified electrophoretically after removal of γ-livetin by precipitation from 37% saturated ammonium sulphate or 20% isopropanol. The α-, β-, and mixed livetins resembled pseudoglobulins in solubility but γ-livetin was unstable and this loss of solubility has, so far, prevented its characterization. Molecular weights determined by light scattering, osmotic pressure, and Archibald sedimentation procedure yielded respectively: 8.7, 7.8, and 6.7 × 104 for α-livetin, and 4.8, 5.0, and4.5 × 104 for β-livetin. Under suitable conditions of sedimentation and electrophoresis, egg yolk has been shown to contain three components having the same behavior as the three livetins of the water-soluble fraction.


Chemosphere ◽  
2010 ◽  
Vol 78 (11) ◽  
pp. 1301-1312 ◽  
Author(s):  
S.M. Rodrigues ◽  
B. Henriques ◽  
J. Coimbra ◽  
E. Ferreira da Silva ◽  
M.E. Pereira ◽  
...  

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