scholarly journals Isolation and Characterization of The Functional Properties of The Major Protein Fraction from Nyamplung (Calophyllum inophyllum)

2014 ◽  
Vol 13 (1) ◽  
pp. 17
Author(s):  
Muhammad Prima Putra ◽  
Pudji Hastuti
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Functional Properties ◽  
Binding Capacity ◽  
Major Protein ◽  
Water Binding ◽  
Water Emulsion ◽  
Calophyllum Inophyllum ◽  
Isolation And Characterization ◽  
Oil Binding

Defatted nyamplung (Calophyllum inophyllum) seeds as by-products of oil extraction is a rich source of protein. In order to evaluate its potential as value-added of nyamplung seeds, nyamplung proteins were isolated by solubilization-precipitation method at pH 3 and 5. The obtaining protein isolates were characterized with respect to their functional properties, including water binding capacity, oil binding capacity, foaming capacity, foaming stability, emulsifying activity, emulsifying stability, gelation capacity, and amino acid composition. The results show that nyamplung protein could be considered as high protein quality because essential amino acids leucine (4.39 %), proline (4.22 %), valine (3.34 %), aspartic acid (3.23 %) and lysine (3.34 %) were found to be the major amino acids. Polar amino acids were higher than non-polar amino acid (1.7 times). With the consequence in higher ratio of water binding capacity to oil binding capacity (2.7 times) and high value of hydrophile-lypophile balance. In general, the isolated protein from precipitation at pH 3 (IP3) was found to have better functional properties than that being precipitated at pH (IP5), and showed excellent in water binding, emulsifying, gelation and foaming properties. In conclusion, IP3 can be utilized as high quality proteins and emulsifier in oil in water emulsion system.

Functional Properties of the Protein Isolate and Major Fractions of Pine Nut Proteins Prepared from the Changbai Mountain in China

2014 ◽  
Vol 881-883 ◽  
pp. 766-775 ◽  
Author(s):  
Dan Wu ◽  
Wei Hong Min ◽  
Jing Sheng Liu ◽  
Li Fang ◽  
Hong Mei Li ◽  
...  
Keyword(s):  
Amino Acids ◽  
Functional Properties ◽  
Protein Solubility ◽  
Essential Amino Acids ◽  
Protein Isolate ◽  
Absorption Capacity ◽  
Changbai Mountain ◽  
Major Protein ◽  
Pine Nut ◽  
A Value

The functional properties of protein isolate and major protein fractions prepared from Changbai Mountain pine nuts were investigated. Albumin, globulin, glutelin, and protein isolates were obtained after the Osborne method and alkaline dissolution and acid precipitation, and protein contents of the fractions are 48.02%, 81.93%, 83.02%, and 89.69%, respectively. For the sulfhydryl contents, albumin is the highest, and glutelin is the lowest. In a disulphide bond, the protein isolate content is the highest with a value of 28.74 μmol/g, and the glutelin content is the lowest with the value of 13.46 μmol/g. For the four kinds of proteins, the essential amino acids in percentage of total amino acids are 31.13%, 34.22%, 30.30%, and 34.54%, respectively. The pH dependent protein solubility profile reveals that the minimum solubility is at pH 5.0, which corresponds to the isoelectric point. Protein isolate has the minimum water absorption capacity with a value of 0.59 ml/g. On the other hand, albumin has the minimum oil absorption capacity with a value of 2.11 ml/g. The emulsifying activity and stability and the foaming activity and stability increased with increasing concentration of four kinds of proteins. SDS-PAGE results showed that these four kinds of proteins have different molecules.

MATHEMATICAL MODELS FOR THE SYNTHESIS OF PLANT-BASED COMPOSITIONS WITH IMPROVED AMINO ACID COMPOSITION

2021 ◽  
Author(s):  
Irina Gaivoronskaya ◽  
Valenitna Kolpakova
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Mathematical Models ◽  
Functional Properties ◽  
Amino Nitrogen ◽  
Essential Amino Acids ◽  
Major Allergen ◽  
Structural Features ◽  
Covalent Bonds ◽  
Pea Protein

The aim of the work was to optimize the process of obtaining multicomponent protein compositions with high biological value and higher functional properties than the original vegetable protein products. Was realized studies to obtain biocomposites on the base of pea protein-oat protein and pea protein-rice protein. Developed composites were enriched with all limited amino acids. For each of the essential amino acids, the amino acid score was 100% and higher. Protein products used in these compositions are not in major allergen list, which allows to use these compositions in allergen-free products and specialized nutrition. To determine biosynthesis parameters for compositions from pea protein and various protein concentrates with the use of transglutaminase enzyme, was studied effect of concentration and exposition time on the amount of amino nitrogen released during the reaction. Decreasing of amino nitrogen in the medium indicated the occurrence of a protein synthesis reaction with the formation of new covalent bonds. Were determined optimal parameters of reaction: the hydromodule, the exposure time, the concentration of EP of the preparation, were obtained mathematical models. Studies on the functional properties of composites, the physicochemical properties of the proteins that make up their composition, and structural features will make it possible to determine the uses in the manufacture of food products based on their ability to bind fat, water, form foam, gels, and etc.

Isolation and characterization of some novel genes of the apolipoprotein A-I family in Japanese eel, Anguilla japonica

2011 ◽  
Vol 6 (4) ◽  
pp. 545-557 ◽  
Author(s):  
Malay Choudhury ◽  
Takahiro Oku ◽  
Shoji Yamada ◽  
Masaharu Komatsu ◽  
Keita Kudoh ◽  
...  
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Consensus Sequence ◽  
Structural Features ◽  
Lipid Binding ◽  
Japanese Eel ◽  
Amino Acid Sequences ◽  
Novel Genes ◽  
Isolation And Characterization

AbstractApolipoproteins such as apolipoprotein (apo) A-I, apoA-IV, and apoE are lipid binding proteins synthesized mainly in the liver and the intestine and play an important role in the transfer of exogenous or endogenous lipids through the circulatory system. To investigate the mechanism of lipid transport in fish, we have isolated some novel genes of the apoA-I family, apoIA-I (apoA-I isoform) 1–11, from Japanese eel by PCR amplification. Some of the isolated genes of apoIA-I corresponded to 28kDa-1 cDNAs which had already been deposited into the database and encoded an apolipoprotein with molecular weight of 28 kDa in the LDL, whereas others seemed to be novel genes. The structural organization of all apoIA-Is consisted of four exons separated by three introns. ApoIA-I10 had a total length of 3232 bp, whereas other genes except for apoIA-I9 ranged from 1280 to 1441 bp. The sequences of apoIA-Is at the exon-intron junctions were mostly consistent with the consensus sequence (GT/AG) at exon-intron boundaries, whereas the sequences of 3′ splice acceptor in intron 1 of apoIA-I1-7 were (AC) but not (AG). The deduced amino acid sequences of all apoIA-Is contained a putative signal peptide and a propeptide of 17 and 5 amino acid residues, respectively. The mature proteins of apoIA-I1-3, 7, and 8 consisted of 237 amino acids, whereas those of apoIA-I4-6 consisted of 239 amino acids. The mature apoIA-I10 sequence showed 65% identity to amino acid sequence of apoIA-I11 which was associated with an apolipoprotein with molecular weight of 23 kDa in the VLDL. All these mature apoIA-I sequences satisfied the common structural features depicted for the exchangeable apolipoproteins such as apoA-I, apoA-IV, and apoE but apoIA-I11 lacked internal repeats 7, 8, and 9 when compared with other members of apoA-I family. Phylogenetic analysis showed that these novel apoIA-Is isolated from Japanese eel were much closer to apoA-I than apoA-IV and apoE, suggesting new members of the apoA-I family.

scholarly journals Modification of structural and functional properties of sunflower 11S globulin hydrolysates

2016 ◽  
Vol 33 (No. 5) ◽  
pp. 474-479 ◽  
Author(s):  
J. Ren ◽  
Ch. Song ◽  
P. Wang ◽  
S. Li ◽  
N. Kopparapu ◽  
...  
Keyword(s):  
Functional Properties ◽  
Emulsion Stability ◽  
Activity Index ◽  
Binding Capacity ◽  
Surface Hydrophobicity ◽  
Foaming Properties ◽  
Hydrolysis Time ◽  
Structural And Functional Properties ◽  
11S Globulin ◽  
Oil Binding

The structural and functional properties such as solubility, emulsifying properties, foaming properties, oil binding capacity, and surface hydrophobicity of sunflower 11S globulin hydrolysates generated by Alcalase at hydrolysis time of 30, 60, 90, and 120 min were evaluated. Circular dichroism analysis showed the hydrolysates possessed a decreased α-helix and β-structure. The hydrolysates exhibited lower surface hydrophobicity. Hydrolysates with shorter hydrolysis time showed the higher emulsifying activity index, but the same emulsion stability and oil binding capacity compared to the original 11S globulin. The longer hydrolysis resulted in lower foaming and emulsion stability. Thus it was demonstrated that by controlling the hydrolysis time of sunflower 11S globulin, hydrolysate with a desirable functional properties can be obtained.

Amino acid sequence of penicillopepsin. I. Isolation and characterization of the chymotryptic peptides

1976 ◽  
Vol 54 (10) ◽  
pp. 872-884 ◽  
Author(s):  
Alexander Kurosky ◽  
Theo Hofmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Acid Protease ◽  
Terminal Region ◽  
Isolation And Characterization

The amino acid sequences of 48 peptides obtained from a chymotryptic digest of the mould acid protease, penicillopepsin (EC 3.4.23.7), have been determined. These peptides established the sequences of 26 unique fragments of up to 28 residues in length. The 28-residue fragment was identified as the N-terminal region. The C-terminal region is represented by a 13-residue fragment. The amino acids contained in these fragments account for some 85% of the residues of the enzyme.

scholarly journals Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: effect of glycosylation on its heparin- and gelatin-binding capabilities

1995 ◽  
Vol 310 (2) ◽  
pp. 615-622 ◽  
Author(s):  
J J Calvete ◽  
K Mann ◽  
W Schäfer ◽  
L Sanz ◽  
M Reinert ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Binding Activity ◽  
Size Exclusion ◽  
Major Protein ◽  
Heparin Binding ◽  
Aggregation State ◽  
Consensus Pattern

We report the complete amino acid sequence of HSP-1, a major protein isolated from stallion seminal plasma or acid extracts of ejaculated spermatozoa. The protein consists of 121 amino acids organized in two types of homologous repeats arranged in the pattern AA‘BB’. Each of the 13-15-residue A-type repeats contains two O-linked oligosaccharide chains. The B-type repeats span 44-47 amino acids each, are not glycosylated, and have the consensus pattern of the gelatin-binding fibronectin type-II module. This domain also occurs in the major bovine seminal plasma heparin-binding proteins PDC-109 (BSP-A1/A2) and BSP-A3. However, unlike the bovine proteins which bind quantitatively to a heparin-Sepharose column, stallion HSP-1 was recovered in both the flow-through and the heparin-bound fractions. Structural analysis showed that the two HSP-1 forms contain identical polypeptide chains which are differently glycosylated. Moreover, size-exclusion chromatography showed that heparin-bound HSP-1 associates with HSP-2, another major seminal plasma protein, into a 90 kDa product, whereas the non-heparin-bound glycoform of HSP-1 is eluted as a monomeric (14 kDa) protein. This suggests that glycosylation may have an indirect effect on the heparin-binding ability of HSP-1 through modulation of its aggregation state. On the other hand, both glycoforms of HSP-1 displayed gelatin-binding activity, indicating that the molecular determinants for binding heparin and gelatin are different.

scholarly journals Evaluation of The Swelling Ability And Water Binding Capacity Of Some Local Plant Consumed In Adamawa State, Nigeria.

2020 ◽  
Vol 45 (5) ◽  
Author(s):  
N.M. Gaila ◽  
M. Buba ◽  
A. Ahmed
Keyword(s):  
Dietary Fiber ◽  
Functional Properties ◽  
Food Systems ◽  
Binding Capacity ◽  
Physicochemical Characteristics ◽  
Water Binding ◽  
Insoluble Dietary Fiber ◽  
Significant Difference ◽  
Local Plant ◽  
Water Swelling

The functional properties are the intrinsic physicochemical characteristics which affect the behavior of ingredient in food systems during processing, manufacturing, storage and preparation etc. Such functional properties include water and oil binding, emulsification capacities, swelling ability and viscosity. This work is aimed at evaluating the swelling Ability and water binding capacities of Spinous Amarantus (alayahon daji) (AA) Senna accedentalis (tasba) (TB), Phyllantus niruri (mace mai goyo) (MC), Hibiscus sabdrariffa (yakuwan daji) (YD) and Leptadenia hastate (yadiya) (YE) which are commonly consumed in our localities with little or no knowledge about their nutritional properties. AOAC method of analysis as outlined by Adabowale was adopted for the analysis with little modifications. All the samples analyzed showed significant water swelling ability with AA and YD showing the highest values of 1.5±0.06 v/g while TB shows the lowest value of 0.5±0.05 v/g. There was a significant difference (p <0.05) in the WBC values (%) obtained for the different plants analyzed. The results revealed that crude AA has the highest value of 12.48±0.82 and YD has the lowest value of 5.50±0.09. Insoluble dietary fiber (IDF) was also extracted from the samples and evaluated for water binding capacity. The Insoluble dietary fibre (IDF) showed WBC values. The highest values 1.54±0.08g/g and lowest 0.94±0.00g/g were obtained MC and YE respectively. All the crude samples showed significant water binding capacity (WBC) than their respective insoluble dietary fiber (IDF). This is as a result of the structural and chemical composition of the crude samples. However, the research has revealed that both the crude and the IDF samples analyzed has therapeutic potentials.

scholarly journals Nutritional Composition, Techno-Functional Properties and Sensory Analysis of Pan Bread Fortified with Kenaf Seeds Dietary Fibre

2021 ◽  
Vol 50 (11) ◽  
pp. 3285-3296
Author(s):  
Nurul Ainaa Farhanah Mat Ramlan ◽  
Salma Malihah Mohammad ◽  
Roselina Karim ◽  
Sharifah Kharidah Syed Muhammad ◽  
Maznah Ismail ◽  
...  
Keyword(s):  
Functional Properties ◽  
Rice Bran ◽  
Wheat Bran ◽  
Sensory Analysis ◽  
Dietary Fibre ◽  
Binding Capacity ◽  
Nutritional Composition ◽  
Water Binding ◽  
Pan Bread ◽  
Kenaf Seed

Kenaf seeds are underutilized source of food with good source of dietary fiber, protein, essential oil, and phytocompounds. The objectives of this study were to determine the nutritional composition of kenaf seeds, the techno-functional properties of kenaf seeds dietary fibre (KSDF), and sensory analysis of pan bread fortified with dietary fibre that was extracted from kenaf seeds. Analyses showed that kenaf seeds are rich in dietary fibre (28.87 g/ 100 g), protein (27.07 g/ 100 g), oil (23.78 g/100 g) and mineral (5.55 g/100 g). The dietary fibre that was extracted through enzymatic hydrolysis (KSDF (EH)) exhibited significantly (p < 0.05) greater water-binding capacity (WBC), oil-binding capacity (OBC) and viscosity than non-enzymatic hydrolyzed kenaf seeds dietary fibre (KSDF (NEH)) and defatted kenaf seed meal (DKSM). Different formulations of bread were prepared by replacing 10% of wheat flour with wheat bran fibre (positive control), rice bran fibre and KSDF, with white bread unfortified with fibre as negative control. Addition of 10% KSDF to bread formulation significantly (p < 0.05) reduced bread height, volume, specific volume, water activity and firmness, and increased proofing time and bread surface colour. Results from the sensory evaluation of the bread samples also showed that KSDF bread was the most acceptable in comparison to rice bran and wheat bran fortified breads. This study shows that kenaf seed has valuable source of dietary fibre with the potential to be used as a functional ingredient in the development of functional breads.

scholarly journals Improvement of Functional Properties of Jack Bean (Canavalia ensiformis) Flour by Germination and Its Relation to Amino Acids Profile

2021 ◽  
Vol 9 (3) ◽  
pp. 812-822
Author(s):  
Bayu Kanetro ◽  
Muhamad Riyanto ◽  
Dwiyati Pujimulyani ◽  
Nurul Huda
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Functional Properties ◽  
Soluble Protein ◽  
Amino Acid Profile ◽  
Jack Bean ◽  
Germination Time ◽  
Bean Flour ◽  
Hydrophobic Amino Acids ◽  
Foaming Capacity

Jack bean as a source of vegetable protein had not been popular. Seed germination had been known to improve its nutritional quality, especially protein and amino acid profile. This study determined the effect of germination on the color, beany flavor, protein content, functional properties, and amino acid profile of jack bean flour. A complete randomized design was used for this experiment. Germination was carried out for 0, 24, 48, and 72 hours. The seed (control) and germinated jack bean flours were analyzed for oil absorption, water absorption, emulsifying and foaming capacities, as well as the soluble protein content to determine the best germination time. Furthermore, the amino acid profile of the jack bean flour produced from the best germination time was analyzed. The results of this study indicated that the total and soluble protein of the seed and germinated jack bean seeds for 0, 24, 48, 60, and 72 hours were 23.30 and 5.95; 22.61 and 7.61; 21.18 and 10.68; 23.26 and 10.22; 23.98 and 10.81%, respectively. Germination of jack bean improved the functional properties. A germination time of 72 hours increased the oil capacity, water absorption capacity, foaming capacity and decreased the emulsion capacity significantly. The hydrophilic and hydrophobic amino acids of the germinated jack bean flour increased to 3.21 and 2.12% of the seed flour, respectively. The increase of the foaming capacity was related to the increase in hydrophobic amino acids of germinated jack bean flour compared to seed flours, that were glycine 1.23 and 1.01; alanine 1.29 and 1.01; valine 1.16 and 1.00; leucine 1.84 and 1.09%, respectively. Germination of jack bean for 72 hours increased significantly the essential amino acids, namely: leucine, lysine, and valine.

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