Modification of structure and functionalities of ginkgo seed proteins by pH-shifting treatment

2021 ◽  
Vol 358 ◽  
pp. 129862
Author(s):  
Weiwei Zhang ◽  
Changqi Liu ◽  
Jing Zhao ◽  
Tianyi Ma ◽  
Zhendong He ◽  
...  
Keyword(s):  
Seed Proteins ◽  
Ph Shifting

GENETIC DIVERSITY IN BAMBARA GROUNDNUT (Vigna subterranean) AS REVEALED BY MOLECULAR WEIGHTS OF THE SEEDS’ PROTEINS

2018 ◽  
Vol 30 (2) ◽  
pp. 19-28
Author(s):  
A. J. Oludare ◽  
J. I. Kioko ◽  
A. A. Akeem ◽  
A. T. Olumide ◽  
K. R. Justina ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Seed Proteins ◽  
Electrophoretic Analysis ◽  
Protein Characterization ◽  
Bambara Groundnut ◽  
Vigna Subterranea ◽  
Phylogenetic Relatedness ◽  
Molecular Weights ◽  
National Centre ◽  
Standard Marker

Nine accessions of Bambara groundnut (Vigna subterranea (L.) Verdc.,syn. Voandzeia subterranea (L.) Thouars ex DC.)  obtained from National Centre for Genetic Resources and Biotechnology (NACGRAB), Ibadan, Oyo state, were assessed for their genetic and phylogenetic relatedness through electrophoretic analysis of the seed proteins. 0.2g of the seeds were weighed and macerated with mortar and pestle in 0.2M phosphate buffer containing 0.133M of acid (NaH2PO4) and 0.067 of base (Na2HPO4) at pH 6.5. Protein characterization with standard marker revealed that the seeds of the nine accessions contained proteins (B.S.A, Oval Albumin, Pepsinogen, Trypsinogen and Lysozyme) with molecular weights ranging from 66kda and above, 45 – 65 kDa, 44 – 33 kda, 32-24 kDa and 23-14 kDa, respectively. The student T-test revealed that accessions B, C, E, F, H and I have molecular weights not significantly different from one another (P<0.05) while samples A, D and G showed significantly different values (P>0.05). All the accessions had at least two proteins and two major bands in common. The study revealed intra-specific similarities and genetic diversity in protein contents among the nine accessions of Bambara groundnut (Vigna subterraranea (L.) Verdc.syn

Identification of Hybrids from Alfalfa Crosses by Electrophoresis of Single Seed Proteins 1

Crop Science ◽  
1972 ◽  
Vol 12 (4) ◽  
pp. 535-537 ◽  
Author(s):  
M. K. Miller ◽  
M. H. Schonhorst ◽  
R. G. McDaniel
Keyword(s):  
Seed Proteins ◽  
Single Seed

Atypical composition of seed proteins in cultivars ofPhaseolus vulgaris L.

1976 ◽  
Vol 18 (3) ◽  
pp. 200-205 ◽  
Author(s):  
Eva Klozová ◽  
J. Kloz ◽  
P. J. Winfield
Keyword(s):  
Seed Proteins

Ginkgo Seed Proteins: Characteristics, Functional Properties and Bioactivities

2021 ◽  
Author(s):  
Wanning Liu ◽  
Minmin Zou ◽  
Yaosong Wang ◽  
Fuliang Cao ◽  
Erzheng Su
Keyword(s):  
Functional Properties ◽  
Seed Proteins

Nutritive value of legume seed proteins

1967 ◽  
Vol 15 (3) ◽  
pp. 439-443 ◽  
Author(s):  
Robert John. Evans ◽  
Selma L. Bandemer
Keyword(s):  
Nutritive Value ◽  
Seed Proteins ◽  
Legume Seed

scholarly journals Antibacterial Peptides Produced by Alcalase from Cowpea Seed Proteins

Antibiotics ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 870
Author(s):  
Ali Osman ◽  
Gamal Enan ◽  
Abdul-Raouf Al-Mohammadi ◽  
Seham Abdel-Shafi ◽  
Samar Abdel-Hameid ◽  
...  
Keyword(s):  
Size Exclusion Chromatography ◽  
Seed Proteins ◽  
Negative Ions ◽  
Size Exclusion ◽  
Ionization Mass ◽  
Bacterial Cells ◽  
Antibacterial Efficiency ◽  
Exclusion Chromatography ◽  
Molecular Masses ◽  
Cowpea Seed

Cowpea seed protein hydrolysates (CPH) were output from cowpea seeds applying alcalase® from Bacillus licheniformis. CPH with an elevated level of hydrolysis was fractionated by size exclusion chromatography (SEC). Both CPH and SEC-portions showed to contain antimicrobial peptides (AMPs) as they inhibited both Gram-positive bacteria, such as Listeria monocytogenes LMG10470 (L. monocytogenes), Listeria innocua. LMG11387 (L. innocua), Staphylococcus aureus ATCC25923 (S.aureus), and Streptococcus pyogenes ATCC19615 (St.pyogenes), and Gram-negative bacteria, such as Klebsiella pnemoniae ATCC43816 (K. pnemoniae), Pseudomonas aeroginosa ATCC26853 (P. aeroginosa), Escherichia coli ATCC25468) (E.coli) and Salmonella typhimurium ATCC14028 (S. typhimurium).The data exhibited that both CPH and size exclusion chromatography-fraction 1 (SEC-F1) showed high antibacterial efficiency versus almost all the assessed bacteria. The MIC of the AMPs within SEC-F1 and CPHs were (25 µg/mL) against P. aeruginosa, E.coli and St. pyogenes. However, higher MICsof approximately 100–150 µg/mL showed for both CPHs and SEC-F1 against both S. aureus and L. innocua; it was 50 µg/mL of CPH against S.aureus. The Electro-spray-ionization-mass-spectrometry (ESI-MS) of fraction (1) revealed 10 dipeptides with a molecular masses arranged from 184 Da to 364 Da and one Penta peptide with a molecular mass of approximately 659 Da inthe case of positive ions. While the negative ions showed 4 dipeptides with the molecular masses that arranged from 330 Da to 373 Da. Transmission electron microscope (TEM) demonstrated that the SEC-F1 induced changes in the bacterial cells affected. Thus, the results suggested that the hydrolysis of cowpea seed proteins by Alcalase is an uncomplicated appliance to intensify its antibacterial efficiency.

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