Multiple Molecular Forms of Avian Aldolases. VI. Enzymatic Properties and Amino Acid Composition of Chicken Liver Aldolase and Comparative Immunochemical Properties

1971 ◽  
Vol 49 (6) ◽  
pp. 658-665 ◽  
Author(s):  
Ronald R. Marquardt
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Chicken Liver ◽  
Molecular Forms ◽  
Ph Optimum ◽  
Muscle Enzyme ◽  
Wide Ph Range ◽  
Mammalian Liver ◽  
Liver And Kidney

Several properties of pure chicken (Gallus domesticus) liver aldolase (fructose-1,6-diphosphate D-glycer-aldehyde-3-phosphate-lyase, EC 4.1.2.13) were determined. The enzyme shows a broad pH optimum peaking around pH 7.7, is stable over a wide pH range, and has a temperature coefficient Q10 of 2.3. The enzyme is stable at 48 °C for 10 min and is almost completely inactivated at 55 °C.The amino acid composition of pure chicken liver aldolase was determined. Its composition was compared with those of chicken muscle and chicken brain aldolases and with the corresponding rabbit aldolase enzymes.Antiserum was prepared against purified chicken liver aldolase and the immunological properties of aldolases from various tissues and species were examined. In the chicken, the antiserum has a very pronounced reaction with liver and kidney aldolases but only a weak cross-reaction with either the brain or the muscle enzyme. The antiserum readily cross-reacts with other avian liver aldolases (turkey and budgerigar) but not with mammalian liver aldolases (rat and rabbit).

Multiple molecular forms of avian aldolases. II. Enzymic properties and amino acid composition of chicken (Gattus domesticus) breast muscle aldolase

1969 ◽  
Vol 47 (5) ◽  
pp. 527-534 ◽  
Author(s):  
Ronald R. Marquardt
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Heat Stability ◽  
Breast Muscle ◽  
Molecular Forms ◽  
Ph Optimum ◽  
Wide Ph Range ◽  
Michaelis Constants ◽  
Ph Range

Several properties of crystalline chicken (Gallus domesticus) breast muscle aldolase (fructose 1,6-diphosphate–D-glyceraldehyde 3-phosphate lyase, EC 4.1.2.13) were determined. The enzyme was found to have a broad pH optimum centered around pH 7.1 and to be remarkably stable over a wide pH range. The temperature coefficient Q10 is 2.6 in the range from 10 to 35 °C. The enzyme is stable at 48 °C for 10 min and almost completely inactivated at 55 °C. The apparent Michaelis constants for fructose 1,6-diphosphate and fructose 1-phosphate were 4.2 × 10−5 M and 1.7 × 10−2 M, respectively. The phosphate inhibitor constant (K1) was 5.5 × 10−3 M.Chicken breast muscle aldolase is similar to the rabbit enzyme in many of the above properties, although there are significant differences in heat stability and amino acid composition.

Effect of maternal diet on the amino acid composition of human uterine fluid

2014 ◽  
Author(s):  
Alexandra Jayne Kermack ◽  
Ying Cheong ◽  
Nick Brook ◽  
Nick Macklon ◽  
Franchesca D Houghton
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Maternal Diet ◽  
Uterine Fluid

Biological Processing of Pea Grain and Secondary Starch Raw Materials to Produce Food and Feed Protein Concentrates

2020 ◽  
Vol 36 (4) ◽  
pp. 49-58
Author(s):  
V.V. Kolpakova ◽  
R.V. Ulanova ◽  
L.V. Chumikina ◽  
V.V. Bessonov
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Mass Fraction ◽  
Geotrichum Candidum ◽  
Protein Concentrate ◽  
Protein Concentrates ◽  
Pea Flour ◽  
Nitrogenous Substances

The goal of the study was to develop a biotechnological process for the production of protein concentrates via bioconversion of pea flour and whey, a secondary product of starch manufacture. Standard and special methods were used to analyze the chemical and biochemical composition of protein concentrates (amino acid, carbohydrate, and fractional) of flour, whey and protein concentrates. It was established that pea flour contains 52.28-57.05% water-soluble nitrogenous substances, 23.04-25.50% salt-soluble, 2.94-4.69% alcohol-soluble compounds, 0-0.61% of soluble glutenine, 6.67-10.40% alkali-soluble glutenine and 5.96-10.86% insoluble sclerotic substances. A mathematical model and optimal parameters of the enzymatic extraction of pea protein with a yield of 65-70% were developed. Ultrasonic exposure increased the yield of nitrogenous substances by 23.16 ± 0.69%, compared with the control without ultrasound. The protein concentrate had a mass fraction of nitrogenous substances of 72.48 ± 0.41% (Nx6.25) and a complete amino acid composition. The microbial conversion by the Saccharomyces cerevisiae 121 and Geotrichum candidum 977 cultures of starch whey which remained after protein precipitation allowed us to obtain feed concentrates from biomass and culture liquid with a protein mass fraction of 61.68-70.48% (Nx6.25). Protein concentrates positively affected the vital signs of rats and their excretory products. A technological scheme was developed to test the complex pea grain and starch whey processing under pilot conditions. pea, protein concentrate, extracts, whey, bioconversion, Geotrichum candidum, Saccharomyces cerevisiae, chemical composition, amino acid composition

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