The purpose of this study was to extract proteins from lentils for
use in bread making to improve nutritional quality of bread. Three
solvents, distilled water, 0.7 M NaCl and 0.05 M NaOH solutions, were
used for extraction. Extractions were done at an alkaline pH near 10
for 30 min....
The purposes for which the fractionation of proteins are
carried out are quite varied and manyfold. However, one of the
more important reasons is that of determining the nature and the
extent of autolysis or proteolysis on the bovine muscle proteins
during post mortem aging. Hence, the development of a...
Ion exchange chromatography methods which have been
developed in recent years appear to offer a sensitive technique that
can be utilized very advantageously in studies on various proteins
and their properties. The application of such a procedure for the
successful fractionation of bovine sarcoplasmic proteins should stimulate
interest and research...
The electrophoretic behavior of sarcoplasmic proteins was
investigated by the use of vertical acrylamide gel electrophoresis.
The first part of the study was concerned with the separation of
sarcoplasmic proteins extracted at different times of post-mortem
aging. Electrophoresis of the sarcoplasmic extracts by the discontinuous
technique, using ten percent acrylamide...
A study was completed to determine the extent of the
protein changes occurring in ground beef stored at
2°C for 10 days.
Sections of semitendinosus muscle were obtained
immediately after the slaughter of three beef animals.
Each section was divided into two equal portions, one of
which was ground and...
The influence of polyphosphates upon the emulsification of
enzymatic hydrolyzates of casein and lactalbumin and upon salt-soluble
meat proteins was determined by a model system in which
oil-in-water emulsions were formed.
Sodium acid pyrophosphate, sodium tripolyphosphate and
sodium hexametaphosphate were mixed together in a weight ratio
of 4:2:4, respectively, to...
Investigations were conducted to determine whether the low molecular weight nitrogen compounds and the extra protein complex of bovine psoas major muscle were altered during a 12-day aging period.
Electrophoretic studies of soluble proteins either before or after gel filtration on Sephadex G-25 columns indicated that the soluble proteins were...