scholarly journals Structural and compositional changes of whey protein and blueberry juice fermented using Lactobacillus plantarum or Lactobacillus casei during fermentation

RSC Advances ◽  
2021 ◽  
Vol 11 (42) ◽  
pp. 26291-26302
Author(s):  
Wang Wen-qiong ◽  
Zhang Jie-long ◽  
Yu Qian ◽  
Zhou Ji-yang ◽  
Lu Mao-lin ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Secondary Structure ◽  
Whey Protein ◽  
Lactobacillus Plantarum ◽  
Lactobacillus Casei ◽  
Schematic Diagram ◽  
Blueberry Juice ◽  
Structure Changes ◽  
Compositional Changes

A possible schematic diagram to show how the secondary structure changes which the whey protein and blueberry juice interaction after Lactobacillus casei or Lactobacillus plantarum fermentation was inferred from the structural analysis results.

scholarly journals Antibacterial Activity Test of Bacteriocin from Lactobacillus brevis, Lactobacillus casei and Lactobacillus plantarum Against Gram Positive Pathogenic Bacteria

2018 ◽  
Vol 3 (3) ◽  
pp. 85
Author(s):  
Novi Permata Sari ◽  
Rafika Sari ◽  
Eka Kartika Untari
Keyword(s):  
Antibacterial Activity ◽  
Lactobacillus Plantarum ◽  
Lactobacillus Casei ◽  
Pathogenic Bacteria ◽  
Heating Temperature ◽  
Lactobacillus Brevis ◽  
Inhibition Zone ◽  
Diffusion Method ◽  
Activity Test ◽  
Ph Range

Bacteriocin is a secondary metabolite product of lactic acid bacteria (LAB) which have an antimicrobial and potentially as a natural preservative. LAB isolates used in this study were Lactobacillus brevis, Lactobacillus casei and Lactobacillus plantarum. This study aimed to determine the antibacterial activity of bacteriocin produced by each isolate of LAB including the influence of pH and heating variation against Bacillus cereus, Bacillus subtilis and Staphylococcus epidermidis. Antibacterial activity test was done by using disc diffusion method. method. Confirmation test using proteolytic enzyme aimed to analyse that the inhibition zone produced from the activity of bacteriocin. The inhibition zone produced from L. brevis, L. casei and L. plantarum against B. cereus were 15.70, 16.43 and 14.50 mm, against B. subtilis were 13.37, 14.10 and 12.53 mm and against S. epidermidis were 11.37, 14.50 and 12.45 mm. The activity of each bacteriocin decreased with the addition of trypsin and catalase, bacteriocin was active in the pH range of 2-10 and heating temperature of 40-121oC. Statistical test showed that the addition of trypsin, catalase and the variation of pH also heating had significant differences (p<0.05) to antibacterial activity produced by bacteriocin from L. brevis, L. casei and L. plantarum. 

scholarly journals Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 359 ◽  
Author(s):  
Usoltsev ◽  
Sitnikova ◽  
Kajava ◽  
Uspenskaya
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Ftir Spectroscopy ◽  
Conformational Changes ◽  
Data Interpretation ◽  
Random Coil ◽  
Helical Conformation ◽  
Structure Changes

Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.

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