Effect of defatted Lagenaria siceraria (Molina) Standley seed flour as a fat replacer on physicochemical, technological, and sensory properties of beef patty.

Defatted Lagenaria siceraria seed flour (DLSSF) was obtained from defatted seed cake, dried, and ground through a sieve of 500 µm and characterized. A 2 × 4 factorial design (two flour hydration rates and four fat substitution rates) was used to produce a low-fat beef patty by replacing fat with DLSSF. Beef kidney fat was used to formulate the control sample. Chemical, physical, technological, sensory, and nutritional characteristics of low-fat beef patties manufactured were evaluated. DLSSF contains mainly protein. As fat replacers, DLSSF induces a significant increase in the pH of the raw and cooked patty, the moisture and protein contents, the cooking yield, the cohesion, chewiness, springiness, and lightness of the cooked beef patty with fat substitution rate. There is a decrease in fat content, total calories, water retention capacity, hardness, and redness of the cooked patty with a fat substitution rate. From the sensory analysis, the substitution of fat improves the acceptability of samples. Based on the overall parameters analyzed, DLSSF containing 60% water can be used to produce low-fat beef patty by replacing fat at 100%. From these results, hydrated DLSSF could be an effective method to solve the problems of noncommunicable diseases related to animal fat consumption.

Anti-listerial peptides from a marine Bacillus velezensis FTL7: production optimization, characterizations and molecular docking studies.

Antimicrobial peptides (AMPs) with potent anti-listerial activity were characterized from a novel marine Bacillus velezensis FTL7. A Box-Behnken statistical experimental design was used to study the combined impact of culture conditions on the production of AMPs by B. velezensis FTL7. The conditions optimized by statistical experimental design were 34.5 °C incubation temperature, 23 h incubation time, and 7.6 initial pH of the medium. AMP purification was performed by ammonium sulphate fractionation and butanol extraction followed by reversed-phase C18 solid-phase extraction. Tricine-SDS-PAGE analysis revealed a peptide with a molecular mass of ~ 6.5 kDa in an active AMPs fraction, whereas the mass spectrometry (MS) analysis showed the presence of AMPs in the mass range of 1-1.6 kDa, along with a 6.5 kDa peptide. Both MS and MS/MS analysis confirmed the AMPs as lipopeptides including surfactin, fengycins and iturin A and a circular bacteriocin amylocyclicin. The minimum inhibitory concentration of these AMPs against L. monocytogenes Scott A was 2.5 µg/mL. Further, the in-silico docking studies showed that the AMPs from B. velezensis FTL7 have high binding energy and stable binding patterns towards L. monocytogenes target proteins. Thus, this new combination of AMPs can serve as an effective food bio-preservative. Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-024-03944-5.

Complete genome sequencing and strain characterization of a novel marine Bacillus velezensis FTL7 with a potential broad inhibitory spectrum against foodborne pathogens.

Bacillus velezensis FTL7 which exhibited potent antimicrobial peptide producing capacity was isolated from a marine sediment sample of the West Coast region, South India, and characterized through experimental and genomic analysis approaches. FTL7 showed potential antimicrobial activity against a broad range of foodborne pathogenic bacteria like Listeria monocytogenes Scott A, Bacillus cereus (ATCC 11778), Salmonella Typhimurium (MTCC 1251), Staphylococcus aureus (ATCC 25923), and Escherichia coli (MTCC 443). It also exhibited strong inhibitory activity against Kocuria rhyzophila (ATCC 934) and Bacillus subtilis subsp. spizizenii (ATCC 6633). Phylogenetic analysis by 16S rRNA gene sequence showed that Bacillus velezensis FTL7 was closely related to B. velezensis LBUM288 (GenBank accession number MG461457) with 100% identity. Whole-genome sequencing of the strain FTL7 was carried out using Illumina sequencing technology to get a better insight into the mechanisms of controlling pathogens by FTL7. The strain FTL7 has a chromosome size of 3849,077 bp with a GC content of 46.56%. The genome consists of 3635 coding sequences, 64 RNA, 59 tRNAs, 5 ncRNAs, and 69 pseudogenes. The presence of genes responsible for the synthesis of non-ribosomal peptides and bacteriocins was identified through genome annotation. Thus, many Bacillus strains, including B. velezensis, have been demonstrated as excellent producers of antimicrobial substances.

Malabar sole (Cynoglossus macrostomus) skin as promising source of type I acid and pepsin solubilized collagens with potential bioactivity.

Fish skin is one of the major non-edible by-products formed during fish processing. This investigation focused on the sustainable valorization of Malabar sole (MS) skin for collagen, which can be utilized as potential alternative of mammalian collagen. Acid and pepsin solubilized collagen (ASC and PSC) were successfully isolated from MS skin with a yield (%, dry weight basis) of 49.5 ± 0.6 and 67.6 ± 0.5, respectively. The isolated collagens were characterized by SDS-PAGE, UV-absorption, DSC, SEM, FTIR spectroscopy, etc., analysis. Both collagens were characterized as type I by SDS-PAGE and the well preserved triple helical structure by FTIR and UV absorption analysis. Denaturation temperature (°C) of the MS skin collagens confirmed by DSC analysis was 33.67 (ASC) and 33.38 (PSC). Both collagens showed high solubility in acidic pH and low NaCl level, and also exhibited a comparatively high degree of fibril-forming capacity. Antioxidant potential of the isolated collagens was confirmed by DPPH (31.4-34.6% at 1.5 mg) and peroxyl (64.6-68.3% at 0.3 mg) radical scavenging assays and observed a dose dependent manner activity. Overall, the results suggested the possibility of using the MS skin as a potential substitute source of realistic type I collagen and also help to reduce issues of fish processing discards. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at (10.1007/s13197-021-04996-8).

Production of egg white hydrolysate by digestion with pineapple bromelain: optimization, evaluation and antioxidant activity study.

Chicken egg white is known to be an excellent source of good quality proteins to make hydrolysate with potential bioactive properties. Enzymatic digestion is a well-known method to produce protein hydrolysates; however, the type of enzyme determines the bioactive potential of the protein hydrolysates due to difference in their catalytic specificity. In this study, process optimization, production and evaluation of whole egg white protein hydrolysate (WEWPH) using pineapple bromelain through the Box-Behnken design were carried out. The design experiment (r 2 = 0.9557) displayed a significant (p < 0.01) effect of pH of egg white (9.0), hydrolysis time (24 h), and enzyme/substrate ratio (3.2 unit/g substrate) on hydrolysis and to form bioactive WEWPH. Antioxidant activity of the WEWPH was confirmed by DPPH radical scavenging assay. Gel filtration chromatography, SDS-PAGE and FTIR spectroscopy analysis of WEWPH revealed the digestion of egg white and the integrity of WEWPH in terms of secondary structure. The WEWPH exhibited strong scavenging activities of DPPH (EC50 = 238.3 µg/ml), ABTS ABTS (EC50 = 54.9 µg/ml), peroxyl (EC50 = 391.6 µg/ml) and superoxide radicals. The WEWPH also displayed reducing power and singlet oxygen quenching activity. These results reveal that the bioactive WEWPH could be a promising ingredient in health food and nutraceuticals. Supplementary Information: The online version contains supplementary material available at 10.1007/s13197-021-05188-0.