De-oiled rice bran (DORB) is a potentially useful by-product of the rice bran oil industry.

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When fish are processed, fish bone becomes a key component of the waste, but to date very few researchers have sought to use fish bone to prepare protein hydrolysates as a means of adding value to the final product. This study, therefore, examines the potential of salmon bone, through an analysis of the benefits of its constituent components, namely fat, moisture, protein, and ash. In particular, the study seeks to optimize the process of enzymatic hydrolysis of salmon bone with trypsin in order to produce angiotensin-I converting enzyme (ACE) inhibitory peptides making use of response surface methodology in combination with central composite design (CCD). Optimum hydrolysis conditions concerning DH (degree of hydrolysis) and ACE-inhibitory activity were initially determined using the response surface model. Having thus determined which of the salmon bone protein hydrolysates (SBPH) offered the greatest level of ACE-inhibitory activity, these SBPH were duly selected to undergo ultrafiltration for further fractionation. It was found that the greatest ACE-inhibitory activity was achieved by the SBPH fraction which had a molecular weight lower than 0.65 kDa. This fraction underwent further purification using RP-HPLC, revealing that the F7 fraction offered the best ACE-inhibitory activity. For ACE inhibition, the ideal peptide in the context of the F7 fraction comprised eight amino acids: Phe-Cys-Leu-Tyr-Glu-Leu-Ala-Arg (FCLYELAR), while analysis of the Lineweaver-Burk plot revealed that the FCLYELAR peptide can serve as an uncompetitive ACE inhibitor. An examination of the molecular docking process showed that the FCLYELAR peptide was primarily able to provide ACE-inhibitory qualities as a consequence of the hydrogen bond interactions taking place between ACE and the peptide. Furthermore, upon isolation form the SBPH, the ACE-inhibitory peptide demonstrated ACE-inhibitory capabilities in vitro, underlining its potential for applications in the food and pharmaceutical sectors.

The aim of this study was to evaluate nutritional composition of China chestnut seeds, Sterculia monosperma Vent. and analyze the physico-chemical properties of flour from the seeds. The results obtained on proximate analysis of China chestnut seeds, S. monosperma, revealed that they contained mostly carbohydrate (73.7% dm), followed by fat (12.0% dm), protein (7.8% dm), fiber (5.5% dm) and ash (1.0% dm). They have a relatively high content of potassium (12.3 mg g(-1) dm) following by phosphorus (2.30 mg g(-1) dm), magnesium (1.87 mg g(-1) dm), sulfur (0.88 mg g(-1) dm) and calcium (0.14 mg g(-1) dm). The fatty acids profile was found to be composed of mainly palmitic (42%) and oleic acids (34%), with general long-chain fatty acids the other significant component by mass (13%). Glutamic acid (17.4%), aspartic acid (12.5%) and arginine (12.5%) were the three major amino acid constituents. The purified seed starch was investigated for its morphological, starch content and physico-chemical properties, such as amylose content, swelling power, solubility and pasting properties. The starch granules were quite round, about 10-15 micron diameter and composed of more than 35% (w/w) of amylose. The pasting properties of flour from the seeds of S. monosperma revealed that gelatinization began at 72.6-73.2 degrees C and the maximum viscosity in the holding period at 95 degrees C was 633 BU. Interestingly and potentially of use, was that the viscosity at the cooling period was more than two-fold higher than that in the holding period.

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It is important to understand the amino acid residues that govern the properties of the binding between antibodies and ligands. We studied the binding of two anti-norfloxacins, anti-nor 132 and anti-nor 155, and the fluoroquinolones norfloxacin, enrofloxacin, ciprofloxacin, and ofloxacin. Binding cross-reactivities tested by an indirect competitive enzyme-linked immunosorbent assay indicated that anti-nor 132 (22–100%) had a broader range of cross-reactivity than anti-nor 155 (62–100%). These cross-reactivities correlated with variations in the numbers of interacting amino acid residues and their positions. Molecular docking was employed to investigate the molecular interactions between the fluoroquinolones and the monoclonal antibodies. Homology models of the heavy chain and light chain variable regions of each mAb 3D structure were docked with the fluoroquinolones targeting the crucial part of the complementarity-determining regions. The fluoroquinolone binding site of anti-nor 155 was a region of the HCDR3 and LCDR3 loops in which hydrogen bonds were formed with TYR (H:35), ASN (H:101), LYS (H:106), ASN (L:92), and ASN (L:93). These regions were further away in anti-nor 132 and could not contact the fluoroquinolones. Another binding region consisting of HIS (L:38) and ASP (H:100) was found for norfloxacin, enrofloxacin, and ciprofloxacin, whereas only ASP (H:100) was found for ofloxacin.

OBJECTIVE To investigate an alternative treatment for bovine mastitis by using Pm11 antimicrobial peptide. SAMPLE 5 bovine mastitis pathogens that were previously isolated from cows affected by either clinical or subclinical mastitis. PROCEDURES The current study introduces Pm11 antimicrobial peptide as an alternative treatment for bovine mastitis. The antibacterial activity of Pm11 was tested against Escherichia coli strain SCM1249, Klebsiella spp strain SCM1282, Staphylococcus aureus strain CM967, Streptococcus agalactiae strain SCM1084, and Streptococcus uberis strain SCM1310 using minimum bactericidal concentrations (MBCs) and time-kill kinetics. The pathogens’ morphological changes were demonstrated using a scanning electron microscope (SEM). The cytotoxicity of Pm11 was assessed using the minimum hemolytic concentration assay. RESULTS MBCs ranged from 2.5 to 10 μM and IC50 ranged from 0.32 to 2.07 μM. Time-kill kinetics at MBC demonstrated that Pm11 reduced viable cell counts of S agalactiae strain SCM1084 and S uberis strain SCM1310 from 105 to 0 CFU/mL within 1 h. E coli strain SCM1249 and S aureus strain CM967 were reduced from 105 to 0 CFU/mL within 4 h. The average Pm11-induced hemolytic activity was < 10% for all Pm11 concentrations tested except at the maximum concentration tested (160 μM: 10.19 ± 2.29%). Based on SEM, Pm11 induced morphological and cellular changes in S aureus and E coli. CLINICAL RELEVANCE Pm11 antimicrobial peptide demonstrated in vitro antibacterial activity against the common bovine mastitis pathogens E coli, S aureus, S agalactiae, and S uberis, except Klebsiella spp, and should be further investigated in vivo.

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