PROTEIN AND NONPROTEIN NITROGEN CONTENTS OF SOME OILSEEDS AND PEAS

1973 ◽  
Vol 53 (3) ◽  
pp. 651-657 ◽  
Author(s):  
R. S. BHATTY ◽  
F. W. SOSULSKI ◽  
K. K. WU
Keyword(s):  
Amino Acids ◽  
Carthamus Tinctorius ◽  
Appreciable Amount ◽  
Amide Nitrogen ◽  
Nonprotein Nitrogen ◽  
Dilute Sodium Hydroxide ◽  
Protein Amino Acids ◽  
Pea Proteins ◽  
High Concentrations ◽  
Nitrogen Contents

Nonprotein nitrogen (NPN) was extracted from seven species of oilseeds and three cultivars of peas (Pisum sativum L.) by three methods. Method 1 was extraction of meal nitrogen with dilute sodium hydroxide and removal of alkali-soluble proteins by trichloroacetic acid (TCA) precipitation. Methods 2 and 3 were extractions of meal nitrogen with 70% ethanol and 1% TCA, respectively. The three solvents extracted vastly different quantities of nitrogen from the meals. Method 3 gave the highest values for NPN followed by methods 1 and 2 in that order. The nitrogen extracted by ethanol was probably the true NPN content of the meals because of the lack of solubility of oilseed and pea proteins in this solvent. The oilseed meals contained more amide nitrogen than the peas. None of the meals contained any significant quantities of nitrate nitrogen. Amino acid analysis of NPN fractions of meals obtained by method 1 showed the oilseed meals and peas to contain, in free state, all the protein amino acids except cystine or an appreciable amount of methionine. The NPN fractions of the meals contained, except in safflower (Carthamus tinctorius L.), high quantities of ammonia, glutamic, and aspartic acids. Safflower NPN fraction contained, in addition to ammonia, more proline and alanine than glutamic and aspartic acids. Mustard (Brassica juncea Coss.) and pea NPN fractions also contained high concentrations of arginine. The other protein amino acids were present in trace or relatively small concentrations. The major conclusion drawn from the data was that the NPN of the seed species used in the study was highly variable and depended on the method and solvent of extraction.

Composition and Pesticide and Herbicide Residue Analysis of Fresh and 40-Year-Old Pasteurized Blue Crab (Callinectes sapidus) Meat

1991 ◽  
Vol 54 (4) ◽  
pp. 298-301 ◽  
Author(s):  
N. R. REDDY ◽  
G. J. FLICK ◽  
G. C. ARGANOSA ◽  
R. W. YOUNG
Keyword(s):  
Amino Acids ◽  
Blue Crab ◽  
Callinectes Sapidus ◽  
Residue Analysis ◽  
Amino Acid Content ◽  
Major Protein ◽  
Herbicide Residue ◽  
Protein Amino Acids ◽  
High Concentrations ◽  
Crab Meat

Fresh and 40-year-old pasteurized blue crab (Callinectes sapidus) meat was analyzed for proximate composition, mineral, heavy metal, and amino acid content and volatiles concentration and possible pesticide and herbicide residue levels. Both fresh and 40-year-old meat had similar proximate compositions. The 40-year-old crab meat contained high levels of iron, manganese, copper, and heavy metals compared to the fresh. Recovery of total amino acids was lower from the 40-year-old meat. Aspartic acid, glutamic acid, leucine, lysine, and arginine were the major protein amino acids of fresh and 40-year-old crab meat. The 40-year-old meat contained high concentrations of ethanol and trimethylamine compared to the fresh. No herbicide residues were detected in either of the products. Decomposition products of pesticide DDT were detected at very low levels only in the 40-year-old crab meat.

CHEMICAL COMPOSITION OF SOME FABA BEAN CULTIVARS

1974 ◽  
Vol 54 (2) ◽  
pp. 413-421 ◽  
Author(s):  
R. S. BHATTY
Keyword(s):  
Sodium Chloride ◽  
Faba Bean ◽  
Protein Solubility ◽  
Amino Nitrogen ◽  
Amide Nitrogen ◽  
Nonprotein Nitrogen ◽  
Total Carbohydrate ◽  
Significant Difference ◽  
Faba Beans ◽  
Nitrogen Contents

Twelve cultivars of faba beans (Vicia faba L.) were analyzed for gross composition, nonprotein nitrogen, amide nitrogen, total free α-amino nitrogen, and for the presence of trypsin inhibitors (TI). In addition, protein solubility characteristics of three faba bean cultivars having low, medium and high protein contents were investigated. The gross composition of the cultivars showed variation only in protein (26 to 35%), total carbohydrate (55 to 61%), and starch (28 to 40%); ether extract, fiber and ash contents were relatively uniform. Nonprotein nitrogen, amide nitrogen, and free α-amino nitrogen contents of the cultivars were also largely similar. About 70 to 90% of the faba bean nitrogen was soluble in dilute sodium hydroxide (pH 12.0), and about 60% in dilute hydrochloric acid (pH 2.0) whereas only 8 to 10% of the nitrogen was soluble at pH 4.0 to 4.5 in a single extraction. Maximum precipitation of the extracted proteins also occurred at pH 4.0. The isoelectric points of faba bean proteins were in the region of pH 4.0 to 4.5. Protein solubility at pH 4.0 was increased threefold by extracting the meals with up to 1.0 M sodium chloride. At neutral pH, sodium chloride concentrations increased protein solubility only by 2 to 4%, whereas at the alkaline pH, protein solubility was decreased by 3 to 5%. Aqueous extracts of the cultivars contained different concentrations of TI. The range in inhibition of the standard trypsin assay was from 2 to 32%, indicating a significant difference in TI activities of the cultivars. None of the cultivars approached soybean (Glycine max Merr.) in its TI activity. The faba bean TI was heat-labile.

NONPROTEIN NITROGEN CONTENTS OF SOME GRAIN LEGUMES

1981 ◽  
Vol 61 (3) ◽  
pp. 515-523 ◽  
Author(s):  
N. W. HOLT ◽  
F. W. SOSULSKI
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Grain Legumes ◽  
Field Pea ◽  
Grain Legume ◽  
Low Molecular Weight ◽  
Field Bean ◽  
Legume Species ◽  
Nonprotein Nitrogen ◽  
Nitrogen Contents

The seeds of nine grain legume species were analyzed for nonprotein nitrogen (NPN), amino acids (AA) in NPN, total nucleic acids and nucleic acid nitrogen (NAN). The range in amounts of low molecular weight NPN as determined by ultrafiltration was 16–75 mg/g N for the nine species. The range in NAN was very small and the average of all species was 23.4 mg/g N or 1.05 mg/g seed. Arginine, alanine, aspartic acid, glutamic acid and glycine were the major AA constituents in the ultrafiltrate NPN of six samples of field pea, fababean and field bean. Twenty percent of the nitrogen (N) of the NPN was in protein AA in fababean while the values were 59–75% for field pea and field bean. The remainder along with the NAN was equal to 3.6–5.7% of the seed N.

THE METABOLISM OF ASCARIS LUMBRICOIDES OVARIES: I. NITROGEN DISTRIBUTION

1955 ◽  
Vol 33 (1) ◽  
pp. 297-306 ◽  
Author(s):  
John K. Pollak ◽  
Donald Fairbairn
Keyword(s):  
Amino Acids ◽  
Ascaris Lumbricoides ◽  
Protein Fraction ◽  
Ammonia Nitrogen ◽  
High Concentration ◽  
Protein Nitrogen ◽  
Amino Amide ◽  
Protein Amino Acids ◽  
High Concentrations ◽  
Reducing Substances

The protein fraction obtained from Ascaris lumbricoides ovaries was analyzed for total, α-amino, and amide nitrogen, as well as amino acids and nucleic acids. In the corresponding non-protein fraction total, α-amino, amide, and ammonia nitrogen, and free amino acids and urea, were determined. Free and protein amino acids were qualitatively similar, but quantitatively dissimilar. Unusually large amounts of proline and alanine were found in the proteins, whereas arginine and methionine could not be identified in protein or free acids. Glutamic acid and alanine comprised one-half of the free acids. Ammonia was present in relatively high concentration, but urea was absent. Much of the non-protein nitrogen was not identified. Ribo- and desoxyribonucleic acids were found in approximately the relative proportions occurring in rat liver, but in much lower concentration. The existence of phosphoproteins was not clearly established. Glycogen and total reducing substances, however, were present initially in high concentrations which decreased markedly when the parasites were maintained in a non-nutrient medium.

THE METABOLISM OF ASCARIS LUMBRICOIDES OVARIES: I. NITROGEN DISTRIBUTION

1955 ◽  
Vol 33 (3) ◽  
pp. 297-306 ◽  
Author(s):  
John K. Pollak ◽  
Donald Fairbairn
Keyword(s):  
Amino Acids ◽  
Ascaris Lumbricoides ◽  
Protein Fraction ◽  
Ammonia Nitrogen ◽  
High Concentration ◽  
Protein Nitrogen ◽  
Amino Amide ◽  
Protein Amino Acids ◽  
High Concentrations ◽  
Reducing Substances

The protein fraction obtained from Ascaris lumbricoides ovaries was analyzed for total, α-amino, and amide nitrogen, as well as amino acids and nucleic acids. In the corresponding non-protein fraction total, α-amino, amide, and ammonia nitrogen, and free amino acids and urea, were determined. Free and protein amino acids were qualitatively similar, but quantitatively dissimilar. Unusually large amounts of proline and alanine were found in the proteins, whereas arginine and methionine could not be identified in protein or free acids. Glutamic acid and alanine comprised one-half of the free acids. Ammonia was present in relatively high concentration, but urea was absent. Much of the non-protein nitrogen was not identified. Ribo- and desoxyribonucleic acids were found in approximately the relative proportions occurring in rat liver, but in much lower concentration. The existence of phosphoproteins was not clearly established. Glycogen and total reducing substances, however, were present initially in high concentrations which decreased markedly when the parasites were maintained in a non-nutrient medium.

scholarly journals Nectar non-protein amino acids (NPAAs) do not change nectar palatability but enhance learning and memory in honey bees

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Daniele Carlesso ◽  
Stefania Smargiassi ◽  
Elisa Pasquini ◽  
Giacomo Bertelli ◽  
David Baracchi
Keyword(s):  
Amino Acids ◽  
Learning And Memory ◽  
Honey Bees ◽  
Feeding Preference ◽  
Memory Retention ◽  
Floral Nectar ◽  
Olfactory Conditioning ◽  
Specific Memory ◽  
Protein Amino Acids ◽  
Valuable Compounds

AbstractFloral nectar is a pivotal element of the intimate relationship between plants and pollinators. Nectars are composed of a plethora of nutritionally valuable compounds but also hundreds of secondary metabolites (SMs) whose function remains elusive. Here we performed a set of behavioural experiments to study whether five ubiquitous nectar non-protein amino acids (NPAAs: β-alanine, GABA, citrulline, ornithine and taurine) interact with gustation, feeding preference, and learning and memory in Apis mellifera. We showed that foragers were unable to discriminate NPAAs from water when only accessing antennal chemo-tactile information and that freely moving bees did not exhibit innate feeding preferences for NPAAs. Also, NPAAs did not alter food consumption or longevity in caged bees over 10 days. Taken together our data suggest that natural concentrations of NPAAs did not alter nectar palatability to bees. Olfactory conditioning assays showed that honey bees were more likely to learn a scent when it signalled a sucrose reward containing either β-alanine or GABA, and that GABA enhanced specific memory retention. Conversely, when ingested two hours prior to conditioning, GABA, β-alanine, and taurine weakened bees’ acquisition performances but not specific memory retention, which was enhanced in the case of β-alanine and taurine. Neither citrulline nor ornithine affected learning and memory. NPAAs in nectars may represent a cooperative strategy adopted by plants to attract beneficial pollinators.

Protection of Italian ryegrass (Lolium multiflorum L.) seedlings from salinity stress following seed priming with L-methionine and casein hydrolysate

2020 ◽  
pp. 1-9
Author(s):  
Keum-Ah Lee ◽  
Youngnam Kim ◽  
Hossein Alizadeh ◽  
David W.M. Leung
Keyword(s):  
Oxidative Stress ◽  
Amino Acids ◽  
Salinity Stress ◽  
Lolium Multiflorum ◽  
Casein Hydrolysate ◽  
Seed Priming ◽  
Germination Percentage ◽  
Italian Ryegrass ◽  
Significant Difference ◽  
Protein Amino Acids

Abstract Seed priming with water (hydropriming or HP) has been shown to be beneficial for seed germination and plant growth. However, there is little information on the effects of seed priming with amino acids and casein hydrolysate (CH) compared with HP, particularly in relation to early post-germinative seedling growth under salinity stress. In this study, Italian ryegrass seeds (Lolium multiflorum L.) were primed with 1 mM of each of the 20 protein amino acids and CH (200 mg l−1) before they were germinated in 0, 60 and 90 mM NaCl in Petri dishes for 4 d in darkness. Germination percentage (GP), radicle length (RL) and peroxidase (POD) activity in the root of 4-d-old Italian ryegrass seedlings were investigated. Generally, when the seeds were germinated in 0, 60 and 90 mM NaCl, there was no significant difference in GP of seeds among various priming treatments, except that a higher GP was observed in seeds of HP treatment compared with the non-primed seeds when incubated in 60 mM NaCl. When incubated in 60 and 90 mM NaCl, seedlings from seeds primed with L-methionine or CH exhibited greater RL (greater protection against salinity stress) and higher root POD activity than those from non-primed and hydro-primed seeds. Under salinity stress, there were higher levels of malondialdehyde (MDA) in the root of 4-d-old Italian ryegrass seedlings, a marker of oxidative stress, but seed priming with CH was effective in reducing the salinity-triggered increase in MDA content. These results suggest that priming with L-methionine or CH would be better than HP for the protection of seedling root growth under salinity stress and might be associated with enhanced antioxidative defence against salinity-induced oxidative stress.

scholarly journals The key amino acids of E protein involved in early flavivirus infection: viral entry

2021 ◽  
Vol 18 (1) ◽  
Author(s):  
Tao Hu ◽  
Zhen Wu ◽  
Shaoxiong Wu ◽  
Shun Chen ◽  
Anchun Cheng
Keyword(s):  
Amino Acids ◽  
Conformational Changes ◽  
Viral Entry ◽  
Envelope Protein ◽  
Cell Attachment ◽  
Envelope Proteins ◽  
Infection Process ◽  
Early Infection ◽  
Protein Amino Acids ◽  
Α Helix

AbstractFlaviviruses are enveloped viruses that infect multiple hosts. Envelope proteins are the outermost proteins in the structure of flaviviruses and mediate viral infection. Studies indicate that flaviviruses mainly use envelope proteins to bind to cell attachment receptors and endocytic receptors for the entry step. Here, we present current findings regarding key envelope protein amino acids that participate in the flavivirus early infection process. Among these sites, most are located in special positions of the protein structure, such as the α-helix in the stem region and the hinge region between domains I and II, motifs that potentially affect the interaction between different domains. Some of these sites are located in positions involved in conformational changes in envelope proteins. In summary, we summarize and discuss the key envelope protein residues that affect the entry process of flaviviruses, including the process of their discovery and the mechanisms that affect early infection.

Ileal digestibility of protein and amino acids of feed peas with different trypsin inhibitor activity in pigs

2000 ◽  
Vol 80 (4) ◽  
pp. 643-652 ◽  
Author(s):  
F. Grosjean ◽  
C. Jondreville ◽  
I. Williatte-Hazouard ◽  
F. Skiba ◽  
B. Carrouée ◽  
...  
Keyword(s):  
Amino Acids ◽  
Trypsin Inhibitor ◽  
Crude Protein ◽  
Trypsin Inhibitor Activity ◽  
Rectal Anastomosis ◽  
Inhibitor Activity ◽  
Ileal Digestibility ◽  
Physical Chemical ◽  
Protein Amino Acids ◽  
Weight Proportion

Ileal digestibility of protein and amino acids was measured in pigs fed 13 round, tannin-free peas samples and related to the following physical, chemical and biological characteristics of these samples: thousand-seed weight, proportion of hulls, starch, fibre, crude protein, ether extract and ash contents, trypsin inhibitor activity and trypsin inhibitor activity per unit of crude protein (TIAP). Each pea sample was included in a diet containing starch, sucrose, minerals and vitamins and fed to four barrows (50 to 100 kg) fitted with an end-to-end ileo-rectal anastomosis. Standardised ileal protein and amino acid digestibilities, except for alanine of peas decreased linearly with increasing TIAP (P < 0.01) and was not affected by fiber content. For example standardized ileal digestibilities values (%) decreased by −0.1975, −0.1617, −0.2171, −0.2630, −0.2029 and −0.3536 per unit of TIAP (expressed in unit of trypsin inhibited per milligram crude protein), respectively, for crude protein and lysine, threonine, methionine, cystine and tryptophan. Key words: Peas, trypsin inhibitor activity, standardised ileal digestibilities, protein, amino acids, pig

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