• Title/Summary/Keyword: proteins and amino acids

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The Effects of Protein and Supplements on Sarcopenia in Human Clinical Studies: How Older Adults Should Consume Protein and Supplements

  • Young Jin Jang
    • Journal of Microbiology and Biotechnology
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    • v.33 no.2
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    • pp.143-150
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    • 2023
  • Sarcopenia is a condition in which muscle mass, strength, and performance decrease with age. It is associated with chronic diseases such as diabetes, cardiovascular disease, and hypertension, and contributes to an increase in mortality. Because managing sarcopenia is critical for maintaining good health and quality of life for the elderly, the condition has sparked concern among many researchers. To counteract sarcopenia, intake of protein is an important factor, while a lack of either protein or vitamin D is a major cause of sarcopenia. In addition, essential amino acids, leucine, β-hydroxy β-methylbutyrate (HMB), creatine, and citrulline are used as supplements for muscle health and are suggested as alternatives for controlling sarcopenia. There are many studies on such proteins and supplements, but it is necessary to actually organize the types, amounts, and methods by which proteins and supplements should be consumed to inhibit sarcopenia. In this study, the efficacy of proteins and supplements for controlling sarcopenia according to human clinical studies is summarized to provide suggestions about how the elderly may consume proteins, amino acids, and other supplements.

Lipid and Protein Constituents of Crotalaria juncea L.

  • Javed, Muhammad Akhtar;Saleem, Muhammad;Yamin, Muhammad;Chaudri, Tanvir Ahmad
    • Natural Product Sciences
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    • v.5 no.3
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    • pp.148-150
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    • 1999
  • Seed lipids and proteins of Crotalaria juncea L were analyzed for fatty acids and amino acids respectively. Gas chromatographic analysis of the oil gave palmitic acid (16.01%), stearic acid (7.29%), oleic acid (14.41%), linoleic acid (54.44%) and linolenic acid (7.86%). The defatted seed cake contained all the essential amino acids except methionine and six non-essential amino acids.

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The Metabolites of a Marine Mollusk Mytilus edulis:- Isolation of Taurine and Compositions of Free Fatty Acids and Free Amino acids-

  • Cho, Yong-Jin;Son, Byeng-Wha;Choi, Hong-Dae
    • Natural Product Sciences
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    • v.1 no.1
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    • pp.5-9
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    • 1995
  • The metabolites of marine mollusk Mytilus edulis were isolated and characterized, revealing the presence of the rare free fatty acids and proteinogenic amino acids together with a non-proteinogenic free amino acid, taurine. The free fatty acids in this organism were particularly interesting for the presence of both unusual n-6 acid [20:4 (n-6)] and triple bond containing acid (2,5-octadecadiynoic acid). In addition to the proteinogenic amino acids commonly found in proteins, non-proteinogenic free amino acid taurine was isolated and the structure was determined by its physicochemical properties. Recently taurine has been given much interest in the molecular level because of diverse biological activities and the medicinal properties. Furthermore, the result of the analyses of analyses of free amino acids showed that glycine, glutamic acid, serine and alanine, which were considered to be related to the taste of this organism, are predominantly present.

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Chemical Composition, Nitrogen Fractions and Amino Acids Profile of Milk from Different Animal Species

  • Rafiq, Saima;Huma, Nuzhat;Pasha, Imran;Sameen, Aysha;Mukhtar, Omer;Khan, Muhammad Issa
    • Asian-Australasian Journal of Animal Sciences
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    • v.29 no.7
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    • pp.1022-1028
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    • 2016
  • Milk composition is an imperative aspect which influences the quality of dairy products. The objective of study was to compare the chemical composition, nitrogen fractions and amino acids profile of milk from buffalo, cow, sheep, goat, and camel. Sheep milk was found to be highest in fat ($6.82%{\pm}0.04%$), solid-not-fat ($11.24%{\pm}0.02%$), total solids ($18.05%{\pm}0.05%$), protein ($5.15%{\pm}0.06%$) and casein ($3.87%{\pm}0.04%$) contents followed by buffalo milk. Maximum whey proteins were observed in camel milk ($0.80%{\pm}0.03%$), buffalo ($0.68%{\pm}0.02%$) and sheep ($0.66%{\pm}0.02%$) milk. The non-protein-nitrogen contents varied from 0.33% to 0.62% among different milk species. The highest r-values were recorded for correlations between crude protein and casein in buffalo (r = 0.82), cow (r = 0.88), sheep (r = 0.86) and goat milk (r = 0.98). The caseins and whey proteins were also positively correlated with true proteins in all milk species. A favorable balance of branched-chain amino acids; leucine, isoleucine, and valine were found both in casein and whey proteins. Leucine content was highest in cow ($108{\pm}2.3mg/g$), camel ($96{\pm}2.2mg/g$) and buffalo ($90{\pm}2.4mg/g$) milk caseins. Maximum concentrations of isoleucine, phenylalanine, and histidine were noticed in goat milk caseins. Glutamic acid and proline were dominant among non-essential amino acids. Conclusively, current exploration is important for milk processors to design nutritious and consistent quality end products.

Food Components of Coho Salmon and Rainbowtrout (은연어와 무지개 송어의 식품성분)

  • 김경삼;최영준
    • The Korean Journal of Food And Nutrition
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    • v.6 no.2
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    • pp.73-80
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    • 1993
  • In order to examine food components of coho salmon and rainbow-trout, We analyzed the composition of protein, amino acids and total lipids. The coho salmon muscle contained about 19.3% of protein with the composition of 29.9% in sarcoplasmic protein, 56.3oA in myofibrillar protein 12.5% alkali soluble protein and 2.6% in stroma. Those of rainbow-trout contained 34.1%, 56.4%, 8.3% and 2.9%, respectively. The sarcoplasmic and myofibrillar protein were composed of 13 subunits in coho salmon, and 16 and 15 subunits in rainbow-trout. Judging from the contents of essential amino acids, both muscle proteins were complete proteins. The most remarkable feature of free amino acids was that a large amount of dipeptide anserine was present with fairly lower levels of 1 methyl histidine, taurine, histidine, alanine and glycine in both muscle extracts. The total fatty acids of coho salmon was composed of 31.49% polyenes, 43.79% monoenes and 24.73% saturates. The composition of total fatty acid of coho salmon muscle was not different from that of rainbow-trout muscle.

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Role of Cel5H protein surface amino acids in binding with clay minerals and measurements of its forces

  • Renukaradhya K. Math;Nagakumar Bharatham;Palaksha K. Javaregowda;Han Dae Yun
    • Applied Microscopy
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    • v.51
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    • pp.17.1-17.10
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    • 2021
  • Our previous study on the binding activity between Cel5H and clay minerals showed highest binding efficiency among other cellulase enzymes cloned. Here, based on previous studies, we hypothesized that the positive amino acids on the surface of Cel5H protein may play an important role in binding to clay surfaces. To examine this, protein sequences of Bacillus licheniformis Cel5H (BlCel5H) and Paenibacillus polymyxa Cel5A (PpCel5A) were analyzed and then selected amino acids were mutated. These mutated proteins were investigated for binding activity and force measurement via atomic force microscopy (AFM). A total of seven amino acids which are only present in BlCel5H but not in PpCel5A were selected for mutational studies and the positive residues which are present in both were omitted. Of the seven selected surface lysine residues, only three mutants K196A(M2), K54A(M3) and K157T(M4) showed 12%, 7% and 8% less clay mineral binding ability, respectively compared with wild-type. The probable reason why other mutants did not show altered binding efficiency might be due to relative location of amino acids on the protein surface. Meanwhile, measurement of adhesion forces on mica sheets showed a well-defined maximum at 69±19 pN for wild-type, 58±19 pN for M2, 53±19 pN for M3, and 49±19 pN for M4 proteins. Hence, our results demonstrated that relative location of surface amino acids of Cel5H protein especially positive charged amino acids are important in the process of clay mineral-protein binding interaction through electrostatic exchange of charges.

Proteomic analysis of amino acid metabolism differences between wild and cultivated Panax ginseng

  • Sun, Hang;Liu, Fangbing;Sun, Liwei;Liu, Jianzeng;Wang, Manying;Chen, Xuenan;Xu, Xiaohao;Ma, Rui;Feng, Kai;Jiang, Rui
    • Journal of Ginseng Research
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    • v.40 no.2
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    • pp.113-120
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    • 2016
  • Background: The present study aimed to compare the relative abundance of proteins and amino acid metabolites to explore the mechanisms underlying the difference between wild and cultivated ginseng (Panax ginseng Meyer) at the amino acid level. Methods: Two-dimensional polyacrylamide gel electrophoresis and isobaric tags for relative and absolute quantitation were used to identify the differential abundance of proteins between wild and cultivated ginseng. Total amino acids in wild and cultivated ginseng were compared using an automated amino acid analyzer. The activities of amino acid metabolism-related enzymes and the contents of intermediate metabolites between wild and cultivated ginseng were measured using enzyme-linked immunosorbent assay and spectrophotometric methods. Results: Our results showed that the contents of 14 types of amino acids were higher in wild ginseng compared with cultivated ginseng. The amino acid metabolism-related enzymes and their derivatives, such as glutamate decarboxylase and S-adenosylmethionine, all had high levels of accumulation in wild ginseng. The accumulation of sulfur amino acid synthesis-related proteins, such as methionine synthase, was also higher in wild ginseng. In addition, glycolysis and tricarboxylic acid cycle-related enzymes as well as their intermediates had high levels of accumulation in wild ginseng. Conclusion: This study elucidates the differences in amino acids between wild and cultivated ginseng. These results will provide a reference for further studies on the medicinal functions of wild ginseng.

The Study in the Composition Changes of Muscle Proteins and Amino Acids in the Hibernant Fish-Mudskipper (Boleophthalmus pectinirostris) before and after Hibernation (동면 전ㆍ후 짱뚱어의 육단백질 및 아미노산 조성의 변화에 관한 연구)

  • 박일웅
    • The Korean Journal of Food And Nutrition
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    • v.16 no.3
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    • pp.209-217
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    • 2003
  • The composition of muscle proteins and free amino acids in the mudskipper (hibernant fish) were investigated before and after hibernation (maturity period: August, hibernation period: November thru. April). It was found that crude proteins were 17.6% in August, 17.5% in November and 16.9% in April, while among the muscle proteins, sarcoplasmic proteins were constituted up to 19.2~20.4%, 58.8~61.3% for myofibrilla proteins, 11.2~13.2% for intracellular proteins and 7.5~8.3% for stroma proteins. Composition changes of the muscle proteins were hardly noted until November but during the hibernation(from Nov. to Apr.) the amount of the sarcoplasmic proteins and the myofibrillar proteins decreased pronouncedly. As for the sarcoplasmic proteins, 14 subunits were found and among them, the amount of 30 kDa and 46 kDa subunits were found to increase slightly in April compared with those in November, while the amount of 35 kDa and 65 kDa subunits were decreased slightly. As for the myofibrilla proteins, 13 subunits were found and detectable changes in their composition were not observed until November but in April the amount of myosin heavy chain was increased by 3%, while the amount of actin decreased by 3% when those are compared with the results in November. The composition of amino acids in the muscle proteins was hardly changed during the observation period. But there were considerable changes of composition of free amino acids. Glycine and alanine were found to be the major free amino acids. The most striking feature was the changes in the glycine and arginine content: the former, which is a dominant free amino acid, was increased by two-fold in April compared with that in August and the latter was increased by two-fold in November and by four-fold in April. It was also found that the amount of essential amino acids (i.e., lysine and histidine) and others (alanine, glutamic acid, serine, aspartic acid and valine) increased significantly during the hibernation period.

Stability Test and Quantitative and Qualitative Analyses of the Amino Acids in Pharmacopuncture Extracted from Scolopendra subspinipes mutilans

  • Cho, GyeYoon;Han, KyuChul;Yoon, JinYoung
    • Journal of Pharmacopuncture
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    • v.18 no.1
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    • pp.44-55
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    • 2015
  • Objectives: Scolopendra subspinipes mutilans (S. subspinipes mutilans) is known as a traditional medicine and includes various amino acids, peptides and proteins. The amino acids in the pharmacopuncture extracted from S. subspinipes mutilans by using derivatization methods were analyzed quantitatively and qualitatively by using high performance liquid chromatography (HPLC) over a 12 month period to confirm its stability. Methods: Amino acids of pharmacopuncture extracted from S. subspinipes mutilans were derived by using O-phthaldialdehyde (OPA) & 9-fluorenyl methoxy carbonyl chloride (FMOC) reagent and were analyzed using HPLC. The amino acids were detected by using a diode array detector (DAD) and a fluorescence detector (FLD) to compare a mixed amino acid standard (STD) to the pharmacopuncture from centipedes. The stability tests on the pharmacopuncture from centipedes were done using HPLC for three conditions: a room temperature test chamber, an acceleration test chamber, and a cold test chamber. Results: The pharmacopuncture from centipedes was prepared by using the method of the Korean Pharmacopuncture Institute (KPI) and through quantitative analyses was shown to contain 9 amino acids of the 16 amino acids in the mixed amino acid STD. The amounts of the amino acids in the pharmacopuncture from centipedes were 34.37 ppm of aspartate, 123.72 ppm of arginine, 170.63 ppm of alanine, 59.55 ppm of leucine and 57 ppm of lysine. The relative standard deviation (RSD %) results for the pharmacopuncture from centipedes had a maximum value of 14.95% and minimum value of 1.795% on the room temperature test chamber, the acceleration test chamber and the cold test chamber stability tests. Conclusion: Stability tests on and quantitative and qualitative analyses of the amino acids in the pharmacopuncture extracted from centipedes by using derivatization methods were performed by using HPLC. Through research, we hope to determine the relationship between time and the concentrations of the amino acids in the pharmacopuncture extracted from centipedes.

Genetic Incorporation of a Phenanthroline-Containing Amino Acid in Escherichia coli

  • Jin, Sunhwa;Lee, Hui-Jung;Lee, Sangyeul;Lee, Hyun Soo
    • Bulletin of the Korean Chemical Society
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    • v.35 no.4
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    • pp.1087-1090
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    • 2014
  • A simple and general method that selectively introduces metal binding sites into a protein can greatly increase the ability to design and biosynthesize artificial metalloproteins. Here, we report the incorporation of a phenanthroline-containing amino acid (Phen-Ala) into proteins in Escherichia coli by using the $tRNA{^{Tyr}}_{CUA}$ and tyrosyl aminoacyl-tRNA synthetase pair (BpyRS) from Methanococcus jannaschii, which was originally developed for a bipyridine-containing amino acid (Bpy-Ala). The incorporation efficiency of BpyRS for Phen-Ala was comparable to that for Bpy-Ala. Because of its high metal-binding ability and characteristic spectral properties, Phen-Ala can be a useful alternative to the existing metal-chelating amino acids for the design and synthesis of artificial metalloproteins.