Starches are valuable biopolymers with several functional and technical applications. Physical and chemical modifications are needed to enhance starch functionality. Modified starches exhibit high ...technological properties in food and non‐food applications. Modified starches are designed to overcome some physicochemical shortcomings of native starches, such as loss of thickening power and viscosity during thermal treatments, storage, retrogradation, and syneresis. Phosphorylation is an effective technique to enhance the functional traits of starches and to modify its physicochemical characteristics (i.e., pasting, gelatinization, and retrogradation). This review summarizes preparation methods, physicochemical properties as well as food and non‐food applications of phosphorylated starch (PS). PSs are being used as a thickener, emulsifier, and stabilizer in food applications. Furthermore, PS can be used as a sedimentation agent for the reclamation of wastes of spent water from the processing of fruits, meat, fishes, vegetables, and brewage. Because PS can substitute and reduce the amount of polyvinyl alcohol, it is used for fixing and sizing in the textile industry. In addition, PS can be used for paper sizing or paper cardboard adhesive coating. It is anticipated that new ventures for PS and their diverse applications will continue to be of a major interest in applied sciences.
Phosphorylation is an effective technique to enhance the functional traits of starches. This review summarizes preparation, physicochemical properties, and applications of phosphorylated starch (PS). It is anticipated that new ventures in PS and their applications will continue to be of interest in applied sciences.
A new preservation approach is presented in this article to prolong the lifetime of raw chicken meat and enhance its quality at 4 °C via coating with highly soluble kidney bean protein hydrolysate. ...The hydrolysates of the black, red, and white kidney protein (BKH, RKH, and WKH) were obtained after 30 min enzymatic hydrolysis with Alcalase (E/S ratio of 1:100, hydrolysis degree 25-29%). The different phaseolin subunits (8S) appeared in SDS-PAGE in 35-45 kD molecular weight range while vicilin appeared in the molecular weight range of 55-75 kD. The kidney bean protein hydrolysates have considerable antioxidant activity as evidenced by the DPPH-scavenging activity and β-carotine-linolenic assay, as well as antimicrobial activity evaluated by disc diffusion assay. BKH followed by RKH (800 µg/mL) significantly (
≤ 0.05) scavenged 95, 91% of DPPH and inhibited 82-88% of linoleic oxidation. The three studied hydrolysates significantly inhibited the growth of bacteria, yeast, and fungi, where BKH was the most performing. Kidney bean protein hydrolysates could shield the chicken meat because of their amphoteric nature and many functional properties (water and oil-absorbing capacity and foaming stability). The quality of chicken meat was assessed by tracing the fluctuations in the chemical parameters (pH, met-myoglobin, lipid oxidation, and TVBN), bacterial load (total bacterial count, and psychrophilic count), color parameters and sensorial traits during cold preservation (4 °C). The hydrolysates (800 µg/g) significantly
≤ 0.05 reduced the increment in meat pH and TVBN values, inhibited 59-70% of lipid oxidation as compared to control during 30 days of cold storage via eliminating 50% of bacterial load and maintained secured storage for 30 days. RKH and WKH significantly (
≤ 0.05) enhanced
*,
* values, thus augmented the meat whiteness and redness, while, BKH increased
* values, declining all color parameters during meat storage. RKH and WKH (800 µg/g) (
≤ 0.05) maintained 50-71% and 69-75% of meat color and odor, respectively, increased the meat juiciness after 30 days of cold storage. BKH, RKH and WKH can be safely incorporated into novel foods.
Delila and Rosea1 anthocyanin accumulation genes were subjected to bioinformatics analysis. Delila protein has 56–69% similarity with different anthocyanin-rich plants, while Rosea1 protein has ...83–87% with anthocyanin-rich plant proteins. This study aimed at transferring Delila and Rosea1 genes from the transgenic Micro-tom tomato cultivar to the Moneymaker tomato cultivar using traditional breeding for enhancing their fruit anthocyanin content. Results of all produced F1 plants of manual hybridization between both cultivars were consistent with the Mendelian inheritance hypothesis. Plants of F2 populations showed a 3:1 Mendelian segregation proportion (75% of plants have anthocyanin pigmentation). Seeds of F2 were individually cultured to get four homozygous lines with anthocyanin accumulation in fruits. The total anthocyanin in the anthocyanin-enriched inbred fruit (3 g/kg DM) represented a relative increase of about 131% of the parent level. The total phenolic compounds in inbred tomato fruits were 54.9 mg/100 g DM referring to a relative increase of about 51% of the respective parent plant. The antioxidant activity of inbred fruit at maturity (m) was 83.5% compared with 91% for TBHQ. The inbred (m) tomato fruit extract reduced the growth of G– bacteria G+ bacteria by 99% and 95%, respectively.
The main target of this work is to discover new protein fractions from natural resources with high antibacterial action. The 7S and 11S globulin fractions, as well as the basic subunit (BS), were ...isolated from lupine seeds (
), chemically characterized, and screened for antibacterial activity against seven pathogenic bacteria. SDS-PAGE revealed molecular weights ranging from 55 to 75 kDa for 7S globulin, 20-37 kD for 11S globulin, and 20 kD for the BS. 11S globulin and the BS migrated faster on Urea-PAGE toward the cathode compared to 7S globulin. FTIR and NMR showed different spectral patterns between the 7S and 11S globulins but similar ones between 11S globulin and the BS. The MICs of the BS were in the range of 0.05-2 μg/mL against
,
,
,
,
,
, and
compared to higher values for 11S globulin. The BS surpassed 11S globulin in antibacterial action, while 7S globulin showed no effect. The MICs of 11S globulin and the BS represented only 5% and 2.5% of the specific antibiotic against
, respectively. Scanning electron microscopy (SEM) demonstrated different signs of cellular deformation and decay in the protein-treated bacteria, probably due to interaction with the bacterial cell wall and membranes. 11S globulin and the BS can be nominated as effective food biopreservatives.
Glycinin, basic subunit and β-conglycinin were isolated from soybean protein isolate and tested for their antimicrobial action against pathogenic and spoilage bacteria as compared to penicillin. The ...three fractions exhibited antibacterial activities equivalent to or higher than penicillin in the next order; basic subunit>glycinin>β-conglycinin with MIC of 50, 100 and 1000μg/mL, respectively. The IC50% values of the basic subunit, glycinin and β-conglycinin against Listeria\monocytogenes were 15, 16 and 695μg/mL, against Bacillussubtilis were 17, 20, and 612μg/mL, and against S. Enteritidis were 18, 21 and 526μg/mL, respectively. Transmission electron microscopy images of L. monocytogenes and S. Enteritidis exhibited bigger sizes and separation of cell wall from cell membrane when treated with glycinin or basic subunit. Scanning electron microscopy of B. subtilis indicated signs of irregular wrinkled outer surface, fragmentation, adhesion and aggregation of damaged cells or cellular debris when treated with glycinin or the basic subunits but not with penicillin. All tested substances particularly the basic subunit showed increased concentration-dependent cell permeation assessed by crystal violet uptake. The antimicrobial action of glycinin and basic subunit was swifter than that of penicillin. The cell killing efficiency was in the following descending order; basic subunit>glycinin>penicillin>β-conglycinin and the susceptibility of the bacteria to the antimicrobial agents was in the next order: L. monocytogenes>B. Subtilis>S. Enteritidis. Adding glycinin and the basic subunit to pasteurized milk inoculated with the three bacteria; L. monocytogenes, B. Subtilis and S. Enteritidis (ca. 5 log CFU/mL) could inhibit their propagation after 16–20days storage at 4°C by 2.42–2.98, 4.25–4.77 and 2.57–3.01 log and by 3.22–3.78, 5.65–6.27 and 3.35–3.72 log CFU/mL, respectively.
► Glycinin and basic subunit have antibacterial action against pathogenic bacteria. ► The antimicrobial action of glycinin and basic subunit is higher than penicillin. ► Glycinin and basic subunit mainly target the cell membrane and cell wall. ► The order of cell killing efficiency was: basic subunit > glycinin > penicillin. ► Contaminating bacteria in stored milk can be inhibited by glycinin and basic subunit.
Summary
The aim of the work was to study the effect of adding cucumber pomace powder (CP) to soft wheat flour used in noodle manufacture. CP is a rich source of minerals and fibres, having high ...contents of polyphenols and flavonoids were 1.6 mg g−1 GAE and 0.65 mg g−1 QE, respectively, besides its capability to inhibit bacterial and fungal growth and to scavenge DPPH˙ (74.44%). The dough rheological properties showed increased extensibility and water absorption but decreased elasticity with adding CP. CP addition significantly increased the mineral and polyphenols content in noodles, but decreased protein and carbohydrates. Noodles enriched with CP 6% have the best organoleptic properties and overall acceptability and were associated with high levels of essential minerals, reduced cooking time by 44% over the control and better nutritional value. No deteriorative changes in dried noodles occurred during 12 months. Cooked noodles enriched with CP 6% significantly reduced the microbial load.
The dry CP‐enriched noodles acquired additional polyphenols, antioxidant activity, antibacterial activity and better rheological properties. The cooked CP‐enriched noodles were characterized by good cooking and physical properties, shorter cooking time, lower energy consumption, less microbial load and better sensorial properties compared to control.
Mycobacterium marinum is an opportunistic pathogen inducing infection in fresh and marine water fish. This pathogen causes necrotizing granuloma like tuberculosis, morbidity and mortality in fish. ...The cell wall-associated lipid phthiocerol dimycocerosates, phenolic glycolipids and ESAT-6 secretion system 1 (ESX-1) are the conserved virulence determinant of the organism. Human infections with Mycobacterium marinum hypothetically are classified into four clinical categories (type I-type IV) and have been associated with the exposure of damaged skin to polluted water from fish pools or contacting objects contaminated with infected fish. Fish mycobacteriosis is clinically manifested and characterized in man by purple painless nodules, liable to develop into superficial crusting ulceration with scar formation. Early laboratory diagnosis of M. marinum including histopathology, culture and PCR is essential and critical as the clinical response to antibiotics requires months to be attained. The pathogenicity and virulence determinants of M. marinum need to be thoroughly and comprehensively investigated and understood. In spite of accumulating information on this pathogen, the different relevant data should be compared, connected and globally compiled. This article is reviewing the epidemiology, virulence factors, diagnosis and disease management in fish while casting light on the potential associated public health hazards.
Heavy metal accumulation and pathogenic bacteria cause adverse effects on aquaculture. The active surface of selenium (Se) nanoparticles can mitigate these effects. The present study used ...Se-resistant
AS12 to fabricate biological Se nanoparticles (Bio-SeNPs). The double-edged Bio-SeNPs were tested for their ability to reduce the harmful effects of heavy metals and bacterial load in Nile tilapia (
) and their respective influences on fish growth, behavior, and health. The Bio-SeNPs have a spherical shape with an average size of 77 nm and high flavonoids and phenolic content (0.7 and 1.9 g g
quercetin and gallic acid equivalents, respectively), resulting in considerable antioxidant and antibacterial activity. The Bio-SeNPs (3-5 μg ml
) in the current study resolved two serious issues facing the aquaculture industry, firstly, the population of pathogenic bacteria, especially
, which was reduced by 28-45% in fish organs. Secondly, heavy metals (Cd and Hg) at two levels (1 and 2 μg ml
) were reduced by 50-87% and 57-73% in response to Bio-SeNPs (3-5 μg ml
). Thus, liver function parameters were reduced, and inner immunity was enhanced. The application of Bio-SeNPs (3-5 μg ml
) improved fish gut health, growth, and behavior, resulting in fish higher weight gain by 36-52% and a 40% specific growth rate, compared to controls. Furthermore, feeding and arousal times increased by 20-22% and 28-53%, respectively, while aggression time decreased by 78% compared to the control by the same treatment. In conclusion, Bio-SeNPs can mitigate the accumulation of heavy metals and reduce the bacterial load in a concentration-dependent manner, either in the fish media or fish organs.
•E. dentata and A. nidulans have been identified with robust growth at 37 °C, and strong PAD productivity.•Purified E. dentata and A. nidulans PADs have molecular mass 41 and 48 kDa, ...respectively.•PADs peptide fingerprints of E. dentata and A. nidulans displayed 18% and 31% similarity to human PAD4.•The orientation of surface trypsinolytic sites on PADs from both fungal isolates were similar.•PADs from both isolates are calcium dependent with participation of serine and cysteine residues on their catalytic sites.
Peptidylarginine deiminases (PADs) are a group of hydrolases, mediating the deimination of peptidylarginine residues into peptidyl-citrulline. Equivocal protein citrullination by PADs of fungal pathogens has a strong relation to the progression of multiple human diseases, however, the biochemical properties of fungal PADs remain ambiguous. Thus, this is the first report exploring the molecular properties of PAD from thermotolerant fungi, to imitate the human temperature. The teleomorph Emericella dentata and anamorph Aspergillus nidulans have been morphologically and molecularly identified, with observed robust growth at 37–40 °C, and strong PAD productivity. The physiological profiles of E. dentata and A. nidulans for PADs production in response to carbon, nitrogen sources, initial medium pH and incubation temperature were relatively identical, emphasizing the taxonomical proximity of these fungal isolates. PADs were purified from E. dentata and A. nidulans with apparent molecular masses 41 and 48 kDa, respectively. The peptide fingerprints of PADs from E. dentata and A. nidulans have been analyzed by MALDI-TOF/MS, displaying a higher sequence similarity to human PAD4 by 18% and 31%, respectively. The conserved peptide sequences of E. dentata and A. nidulans PADs displayed a higher similarity to human PAD than A. fumigatus PADs clade. PADs from both fungal isolates have an optimum pH and pH stability at 7.0–8.0, with putative pI 5.0–5.5, higher structural denaturation at pH 4.0–5.5 and 9.5–12 as revealed from absorbance at λ280nm. E. dentata PAD had a higher conformationally thermal stability than A. nidulans PAD as revealed from its lower Kr value. From the proteolytic mapping, the orientation of trypsinolytic recognition sites on the PADs surface from both fungal isolates was very similar. PADs from both isolates are calcium dependent, with participation of serine and cysteine residues on their catalytic sites. PADs displayed a higher affinity to deiminate the peptidylarginine residues with a feeble affinity to work as ADI. So, PADs from E. dentata and A. nidulans had a relatively similar conformational and kinetic properties. Further molecular modeling analysis are ongoing to explore the role of PADs in citrullination of human proteins in Aspergillosis, that will open a new avenue for unraveling the vague of protein-protein interaction of human A. nidulans pathogen.
As antibiotics cannot inhibit multidrug-resistant bacteria (MDR), continuous research is mandatory to find other antibacterials from natural resources. Native legume proteins and their modified forms ...exhibited broad spectra of high antimicrobial activities. Sixteen bacterial isolates were mapped for antibiotic resistance, showing resistance in the range of (58-92%) and (42-92%) in the case of the Gram-negative and Gram-positive bacteria, respectively. White native Phaseolus vulgaris protein (NPP) was isolated from the seeds and methylated (MPP). The MIC range of MPP against 7 MDR bacteria was 10-25 times lower than NPP and could (1 MIC) considerably inhibit their 24 h liquid growth. MPP showed higher antibacterial effectiveness than Gentamycin, the most effective antibiotic against Gram-positive bacteria and the second most effective against Gram-negative bacteria. However, MPP recorded MICs against the seven studied MDR bacteria in the 1-20 µg/mL range, the same for Gentamycin. The combination of Gentamycin and MPP produced synergistic effects against the seven bacteria studied, as confirmed by the Transmission Electron Microscopic images. The antimicrobial activity of MPP against the seven MDR bacteria remained stable after two years of cold storage at 8-10 °C as contrasted to Gentamycin, which lost 20-72% of its antimicrobial effectiveness.
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