Bacteriophages: a potential game changer in food processing industry.

In the food industry, despite the widespread use of interventions such as preservatives and thermal and non-thermal processing technologies to improve food safety, incidences of foodborne disease continue to happen worldwide, prompting the search for alternative strategies. Bacteriophages, commonly known as phages, have emerged as a promising alternative for controlling pathogenic bacteria in food. This review emphasizes the potential applications of phages in biological sciences, food processing, and preservation, with a particular focus on their role as biocontrol agents for improving food quality and preservation. By shedding light on recent developments and future possibilities, this review highlights the significance of phages in the food industry. Additionally, it addresses crucial aspects such as regulatory status and safety concerns surrounding the use of bacteriophages. The inclusion of up-to-date literature further underscores the relevance of phage-based strategies in reducing foodborne pathogenic bacteria's presence in both food and the production environment. As we look ahead, new phage products are likely to be targeted against emerging foodborne pathogens. This will further advance the efficacy of approaches that are based on phages in maintaining the safety and security of food.

Nanotechnology impacting probiotics and prebiotics: a paradigm shift in nutraceuticals technology.

This is proven for a long that the incorporation of probiotics and prebiotics in diet exhibits beneficial effects on intestinal and intrinsic health. Nevertheless, this may encounter loss of vitality all along the absorption in the gastrointestinal tract, leading to meager intestinal delivery of probiotic active ingredients. In recent times, nanotechnology has been passionately used to escalate the bioavailability of active ingredients. Versatile forms of nanoparticles (NPs) are devised to be used with probiotics/prebiotics/synbiotics or their different combinations. The NPs currently in trend are constituted of distinctive organic compounds like carbohydrates, proteins, fats, or inorganics such as oxides of silver and titanium or magnesium etc. This review critically explicates the emerging relationship of nanotechnology with probiotics and prebiotics for different applications in neutraceuticals. Here in this review, formulations of nanoprobiotics and nanoprebiotics are discussed in detail, which behave as an effective drug delivery system. In addition, these formulations exhibit anti-cancerous, anti-microbial, anti-oxidant and photo-protective properties. Limited availability of scientific research on nanotechnology concerning probiotics and prebiotics implies dynamic research studies on the bioavailability of loaded active ingredients and the effective drug delivery system by including the safety issues of food and the environment.

Rheological and microstructural characteristics of low molecular weight glutenin subunits of commercial wheats.

A study was conducted on the effects occurred in rheological properties of base flour dough by the addition of gluten, glutenin and purified low molecular weight glutenin subunits (LMW-GS) using a 4 g sample Microdoughlab (MDL). Incorporation of these elements brought about a significant increase in the dough strength in the order of LMW-GS < gluten < glutenin. LMW-GS from variety C 306 brought a decrease in the dough development time (DDT; 2.03 min), dough stability (DS; 3 min) and peak energy (EP; 2.90 Wh/kg) values. On the contrary, the effects of LMW-GS extracted from variety PBW 550 were more strong as indicated by an increase in DDT (2.75 min), DS (3.30 min) and EP (4.20 Wh/kg). The alterations in the microstructure of dough by the inclusion of gluten, glutenin and LMW-GS, which lacks resemblance among different samples, were contemplated subjecting it to Scanning Electron Microscopy (SEM).

Extraction and purification of low molecular weight glutenin subunits using size exclusion chromatography.

Crude glutenin of commercial Indian wheat varieties was fractionated into high molecular weight glutenin subunits (HMW-GS) and low molecular weight glutenin subunits (LMW-GS) by employing size-exclusion chromatography (SEC). The SEC profile of glutenins obtained with different buffers were discriminated effectively with respect to the quality of the proteins eluted in each peak. The most efficient separation of LMW-GS was achieved using 3 M urea (pH 5.5) buffer under unreduced conditions. The chromatogram was segregated predominantly into three peaks with varied molecular weights as determined by SDS-PAGE. Peak I corresponded to a mixture of HMW-GS and LMW-GS (Mw 100-30 kDa). Peak II enclosed LMW-GS specifically with molecular weights in the range of 45-35 kDa. Lastly, a mixture of proteins associated with LMW-GS (Mw < 35 kDa) were eluted in peak III. SEC proved to be a valuable tool in purifying LMW-GS in a functionally active state.

Quantification and varietal variation of low molecular weight glutenin subunits (LMW-GS) using size exclusion chromatography.

Crude glutenin of four commercial wheat varieties viz. C 306, HI 977, HW 2004 and PBW 550 of diverse origin and breadmaking quality were fractionated by size-exclusion chromatography into three fractions of decreasing molecular weights. The relative quantity of peak II, containing LMW-GS specifically, varied considerably among the varieties as reflected from their discrete SEC profiles. The area % of peak II, containing protein of interest, was maximal for C 306 (22.08%) followed by PBW 550 (15.86%). The least proportion of LMW-GS were recovered from variety HW 2004 (9.68%). As the concentration of the sample extract injected to the column increased, the resolution of the peak declined in association with the slight shifting of retention time to the higher values. The best results were obtained for variety C 306 at 100 mg protein concentration with 3 M urea buffer. Consequently, the optimized conditions for purification of LMW-GS in appreciable amounts using SEC were established.

Fractionation of unreduced gluten proteins on SEC and their relationship with cookie quality characteristics.

The size distribution assessment of unreduced wheat gluten proteins of commercial Indian wheat varieties was examined using Size-Exclusion Fast Protein Liquid Chromatography. Elution profiles were fractionated into five peaks, with the molecular weights of eluting peaks as 130-30, 55-20, 28-10 and <10 kDa (IV and V), respectively. Peak I (glutenins) and II (gliadins) exhibited contrary results with AWRC (r = 0.928** and r = -0.831**), R/E ratio (r = 0.745** and r = -0.869**), gluten index (r = 0.959** and r = -0.994**), gliadin/glutenin ratio (r = -0.952** and r = 0.948**), dough development time (r = 0.830** and r = -0.930**), dough stability (r = 0.901** and r = -0.979**) and dough weakening (r = -0.969** and r = 0.986**). Significant statistical correlation was also observed for peak I and II with cookie hardness (r = 0.948** and r = -0.924**) and cookie spread (r = -0.837** and r = -0.743**) respectively. Peak III, IV and V occupied a minor fraction of whole and did not exhibit a statistically significant correlation with any of the quality parameters.

Evaluation of molecular weight distribution of unreduced wheat gluten proteins associated with noodle quality.

Unreduced gluten proteins of Indian wheat varieties viz.C306, DBW16, HI977 and HW2004 were separated using size-exclusion chromatography (SEC). Statistical correlation of area % of eluted peaks with properties of flour, dough and noodles was elucidated. Chromatograms of gluten proteins were classified primarily into five peaks in decreasing molecular size range and relative proportion were expressed in terms of area % of individual peaks which depicts the quantitative variation in protein eluted at different retention times. Cooking time and cooked weight of noodles depicted positive correlation with peak I and negative correlation with peak II which predominantly composed of glutenins and gliadins, respectively. Oil uptake and cooking loss were negatively association with peak I and positively with peak II. Noodle hardness, springiness, cohesiveness and chewiness were positively correlated with peak I and negatively to peak II, though adhesiveness was unaffected by SEC eluted peaks statistically.

Relationship of molecular weight distribution profile of unreduced gluten protein extracts with quality characteristics of bread.

A statistical correlation was established among the molecular weight distribution patterns of unreduced gluten proteins and physicochemical, rheological and bread-making quality characteristics of wheat varieties. Size exclusion chromatography fractionated the gluten proteins apparently into five peaks. Peak I signified glutenins (30-130kDa), peak II as gliadins (20-55kDa), peak III as very low molecular weight monomeric gliadins (10-28kDa), peak IV and V, collectively, as albumins and globulins (<10kDa). Peaks I and II had appreciable effects on dough development time (r=0.830(∗∗) and r=-0.930(∗∗)) and dough stability (r=0.901(∗∗) and r=-0.979(∗∗)). Peak I was associated with R/E ratio (r=0.745(∗∗)), gluten index (r=0.959(∗∗)), and gliadin/glutenin ratio (r=-0.952(∗∗)), while peak II influenced inversely as expected. Peak I exhibited positive statistical significance with bread loaf volume (r=0.848(∗∗)); however, peak II had negative (r=-0.818(∗∗)) impact. Bread firmness increased with increment in peak II (r=0.625(∗∗)), and decreased with accretion in peak I (r=-0.623(∗∗)).

Assessment of molecular weight distribution of wheat gluten proteins for chapatti quality.

Size exclusion chromatography (SEC) was used to characterize molecular weight distribution pattern of gluten proteins of four Indian commercial wheat varieties in order to elucidate their influence on flour physicochemical, dough rheology and quality characteristics of chapatti. SEC profile of a wheat variety was segregated into five domains: peak I (130-30 kDa; glutenins), peak II (55-20 kDa; gliadins), peak III (28-10 kDa; low molecular weight gliadins), peak IV and V (<10 kDa; albumins and globulins). SEC results indicated that R/E ratio (r=0.745(∗∗) and r=-0.869(∗∗)), gluten index (r=0.959(∗∗) and r=-0.994(∗∗)), dough development time (r=0.830(∗∗) and r=-0.930(∗∗)) and dough stability (r=0.901(∗∗) and r=-0.979(∗∗)) were positively and negatively altered by peak I and II, respectively. Peak I (r=0.879(∗∗) and r=-0.981(∗∗)) and peak II (r=-0.744(∗∗) and r=0.995(∗∗)) substantially influenced the chapatti hardness and overall score, respectively.