scholarly journals Antioxidant and chelating activities from Lion fish (Pterois volitans L.) muscle protein hydrolysates produced by in vitro digestion using pepsin and pancreatin.

2020 ◽  
pp. 62
Author(s):  
Luis Chel-Guerrero ◽  
David Cua-Aguayo ◽  
David Betancur-Ancona ◽  
Azucena Chuc-Koyoc ◽  
Irma Aranda-González ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Acid Content ◽  
Amino Acid Content ◽  
Fish Muscle ◽  
Degree Of Hydrolysis ◽  
Chelating Activity ◽  
Freeze Dried ◽  
Sds Page

The aim of the present research was to determine the antioxidant, and Cu2+ and Fe2+ chelating activities, amino acid content and estimated molecular weight of proteins and peptides from lion fish muscle-derived hydrolysates obtained by enzymatic hydrolysis with pepsin and pancreatin. The fillets were freeze-dried and hydrolysis was performed, taking aliquots at different times. The degree of hydrolysis, antioxidant activity against ABTS+ and DPPH, Cu2+ and Fe2+ chelating activity, as well as molecular weight estimated by SDS-PAGE and amino acid content by HPLC was determined. The highest degree of hydrolysis (DH) was at 180 min (37.75%). SDS-PAGE showed proteins with an estimated molecular weight of 45,259 and 42,487 Da, which could be associated with myofibrillar proteins. The progressive degradation of proteins by enzymes was also observed, detecting polypeptides with a EMW of 5,988 and 4,954 Da in the most representative hydrolysates. The H40 hydrolysate exhibited the highest ABTS and DPPH radical depuration activity, with values of 107.31 mM/mg protein and 54.27%, respectively. The iron and copper chelating activity was related to DH, since the highest values of iron and copper chelating activity were obtained in hydrolysates H120 and H140, with 90.83% chelation of Cu2+ and 56.33% chelation of Fe2+, respectively with no significant differences compared to subsequent times. In addition, the antioxidant and chelating activities were possibly related to Trp, Cys, Lys, Pro and Arg content. Lion fish muscle hydrolysates could be a potential source of functional ingredients due to their in vitro antioxidant and chelating activity.

Amino Acid Content and In Vitro Protein Quality of Different Corn Varieties

1985 ◽  
pp. 421-437
Author(s):  
Samy Fangus Sharobeem ◽  
Radomir Lásztity ◽  
Máté Hidvégi ◽  
András Salgó ◽  
Livia Simon-Sarkadi
Keyword(s):  
Amino Acid ◽  
Acid Content ◽  
Protein Quality ◽  
Amino Acid Content ◽  
Vitro Protein

Trans-tegumental absorption of L-alanine and L-leucine by a monogenean, Diclidophora merlangi

Parasitology ◽  
1978 ◽  
Vol 76 (1) ◽  
pp. 29-37 ◽  
Author(s):  
D. W. Halton
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Sea Water ◽  
Low Molecular Weight ◽  
Acid Uptake ◽  
Neutral Amino Acids ◽  
Freeze Dried ◽  
Significant Difference

SummaryAn in vitro investigation has been made of the relative roles of the gut and tegument in the absorption of the neutral amino acids L-alanine and L-leucine by a marine fish-gill parasite, Diclidophora merlangi. The use of ligatures to preclude oral ingestion of trace-labelled medium has proved inadequate, invariably damaging the tegument, as revealed by stereoscan electron microscopy, and resulting in artifactual levels of absorption. Three alternative procedures have given consistently reliable data on the route of entry of low molecular weight substrates. (1) Ultrastructural examination of worms previously incubated in electron-dense cationic tracers has shown that, in vitro, there is no oral intake of sea water. (2) The suspending of worms in trace-labelled medium with the mouth out of the medium and comparing amino acid uptake with that of worms totally immersed in medium has revealed no statistically significant difference in the absorption levels. (3) Application of section (freeze-dried) auto-radiography to detect diffusible isotope has demonstrated directly transtegumental absorption of a neutral amino acid. It is concluded from these experiments that Diclidophora has a tegumental transport system for absorbing certain neutral amino acids, and whilst, clearly, the worm is sanguinivorous and digests blood in a well-developed gut, it may also be capable of supplementing this diet with low molecular weight organic nutrient absorbed directly from sea water via the tegument.

scholarly journals Conformational differences between two wheat (Triticum aestivum) ‘high-molecular-weight’ glutenin subunits are due to a short region containing six amino acid differences

1989 ◽  
Vol 263 (3) ◽  
pp. 837-842 ◽  
Author(s):  
A P Goldsbrough ◽  
N J Bulleid ◽  
R B Freedman ◽  
R B Flavell
Keyword(s):  
Molecular Weight ◽  
Triticum Aestivum ◽  
Amino Acid ◽  
High Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Sequences ◽  
Glutenin Subunits ◽  
Sds Page ◽  
Hmw Glutenin

‘High-molecular-weight’ (HMW, high-Mr) glutenin subunits are protein constituents of wheat (Triticum aestivum) seeds and are responsible in part for the viscoelasticity of the dough used to make bread. Two subunits, numbered 10 and 12, are the products of allelic genes. Their amino acid sequences have been derived from the nucleic acid sequences of the respective genes. Subunit 10 has fewer amino acids than subunit 12, but migrates more slowly on SDS/PAGE (polyacrylamide-gel electrophoresis). This anomaly is due to between one and six of the amino acid differences between the subunits, localized towards the C-terminal end of the proteins. This has been established by making chimaeric genes between the genes for subunits 10 and 12, transcribing and translating them in vitro and analysing the products by SDS/PAGE. The postulated conformational differences between subunits 10 and 12 are discussed in relation to current hypotheses for the structure of HMW glutenin subunits.

scholarly journals The Amino Acid Content of Fish Muscle Protein.

1954 ◽  
Vol 20 (6) ◽  
pp. 520-524 ◽  
Author(s):  
Kei-ichiroh SUGIMURA ◽  
Hirokadzu TAIRA ◽  
Naoji HOSHINO ◽  
Harue EBISAWA ◽  
Taroh NAGAHARA
Keyword(s):  
Amino Acid ◽  
Acid Content ◽  
Muscle Protein ◽  
Amino Acid Content ◽  
Fish Muscle

scholarly journals Development of Isocratic RP-HPLC Method for Separation and Quantification of L-Citrulline and L-Arginine in Watermelons

2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Rasdin Ridwan ◽  
Hairil Rashmizal Abdul Razak ◽  
Mohd Ilham Adenan ◽  
Wan Mazlina Md Saad
Keyword(s):  
Amino Acid ◽  
Acid Content ◽  
Citrullus Lanatus ◽  
Amino Acid Content ◽  
Hplc Method ◽  
Efficient Separation ◽  
Rp Hplc ◽  
Mobile Phases ◽  
Freeze Dried ◽  
Arginine Concentration

Watermelons(Citrullus lanatus)are known to have sufficient amino acid content. In this study, watermelons grown and consumed in Malaysia were investigated for their amino acid content, L-citrulline and L-arginine, by the isocratic RP-HPLC method. Flesh and rind watermelons were juiced, and freeze-dried samples were used for separation and quantification of L-citrulline and L-arginine. Three different mobile phases, 0.7% H3P04, 0.1% H3P04, and 0.7% H3P04 : ACN (90 : 10), were tested on two different columns using Zorbax Eclipse XDB-C18and Gemini C18with a flow rate of 0.5 mL/min and a detection wavelength at 195 nm. Efficient separation with reproducible resolution of L-citrulline and L-arginine was achieved using 0.1% H3P04on the Gemini C18column. The method was validated and good linearity of L-citrulline and L-arginine was obtained withR2= 0.9956,y=0.1664x+2.4142andR2=0.9912,y=0.4100x+3.4850, respectively. L-citrulline content showed the highest concentration in red watermelon of flesh and rind juice extract (43.81 mg/g and 45.02 mg/g), whereas L-arginine concentration was lower than L-citrulline, ranging from 3.39 to 11.14 mg/g. The isocratic RP-HPLC method with 0.1% H3P04on the Gemini C18column proved to be efficient for separation and quantification of L-citrulline and L-arginine in watermelons.

scholarly journals Properties of caldesmon isolated from chicken gizzard

1985 ◽  
Vol 230 (3) ◽  
pp. 695-707 ◽  
Author(s):  
P K Ngai ◽  
M P Walsh
Keyword(s):  
Amino Acid ◽  
Light Chain ◽  
Cyclic Nucleotide ◽  
Acid Content ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Amino Acid Content ◽  
Cyclic Nucleotide Phosphodiesterase ◽  
Chicken Gizzard

Chicken gizzard smooth muscle contains two major calmodulin-binding proteins: caldesmon (11.1 microM; Mr 141 000) and myosin light-chain kinase (4.6 microM; Mr 136 000), both of which are associated with the contractile apparatus. The amino acid composition of caldesmon is distinct from that of myosin light-chain kinase and is characterized by a very high glutamic acid content (25.5%), high contents of lysine (13.6%) and arginine (10.3%), and a low aromatic amino acid content (2.4%). Caldesmon lacked myosin light-chain kinase and phosphatase activities and did not compete with either myosin light-chain kinase or cyclic nucleotide phosphodiesterase (both calmodulin-dependent enzymes) for available calmodulin, suggesting that calmodulin may have distinct binding sites for caldesmon on the one hand and myosin light-chain kinase and cyclic nucleotide phosphodiesterase on the other. Consistent with the lack of effect of caldesmon on myosin phosphorylation, caldesmon did not affect the assembly or disassembly of myosin filaments in vitro. As previously shown [Ngai & Walsh (1984) J. Biol. Chem. 259, 13656-13659], caldesmon can be reversibly phosphorylated. The phosphorylation and dephosphorylation of caldesmon were further characterized and the Ca2+/calmodulin-dependent caldesmon kinase was purified; kinase activity correlated with a protein of subunit Mr 93 000. Caldesmon was not a substrate of myosin light-chain kinase or phosphorylase kinase, both calmodulin-activated protein kinases.

Amino acid content of water-stressed plantlets of Populus tremuloides clones in relation to clonal susceptibility to Hypoxylon mammatum in vitro

1990 ◽  
Vol 68 (1) ◽  
pp. 26-29 ◽  
Author(s):  
R. R. Bélanger ◽  
P. D. Manion ◽  
D. H. Griffin
Keyword(s):  
Amino Acids ◽  
Water Stress ◽  
Amino Acid ◽  
Populus Tremuloides ◽  
Acid Content ◽  
Amino Acid Content ◽  
Susceptibility To Infection ◽  
Hypoxylon Mammatum ◽  
Inoculation Study

Plantlets from five clones of Populus tremuloides were cultured in media at three different osmotic potentials to assess the effects of water stress on amino acid content. Differences in amino acid content were then related to differences in susceptibility (determined in a previous study) of clones to Hypoxylon mammatum. Changes in amino acid concentrations varied among the amino acids. Alanine, arginine, asparagine, glutamine, glutamate, and proline increased generally but not consistently among all clones. Comparisons among the clones for these six amino acids showed significant variations. Proline, which has been shown to accelerate radial growth of H. mammatum more than other amino acids, increased progressively with increased water stress in all clones. Levels of proline among the clones were correlated (r = 0.89) with susceptibility to infection and colonization of the clones by H. mammatum. Alanine and glutamine were also similarly correlated with infection rating. However, one clone, which grew poorly in culture, did not show this relationship. In comparison with the other clones, it had low levels of all amino acids, which did not increase significantly in response to water stress. Yet in the inoculation study, it had the highest infection rating at all stress levels, suggesting that other stress-induced factors are also important. These results suggest that nitrogen status of some aspen clones under water stress may increase their susceptibility to hypoxylon canker.

Sign in / Sign up

Export Citation Format

Share Document