The significant increase in chicken meat consumption calls for the development of green technologies to efficiently utilize chicken by-products, such as chicken hearts. This study aimed to characterize and compare the physico-chemical, techno-functional and antioxidant properties of protein hydrolysates derived from chicken heart fermented with Lactobacilli bacteria. Freeze-dried hydrolysates 2Hh16 (2 × 107 cfu/ml Lactobacillus helveticus-NCDC-292, 16 h fermentation) and 2Hp16 (2 × 107 cfu/ml Lactiplantibacillus plantarum-NCDC-025, 16 h fermentation) were analyzed and compared to freeze-dried raw chicken heart powder (Hc). The hydrolysates, whose molecular weight were in the range of 5–20 kDa demonstrated improved soluble protein content and degree of hydrolysis (
This study evaluated the prebiotic and synbiotic potential of green banana (GBF), jackfruit (JFF), sweet potato (SPF), and cassava (CSF) flours in skim milk fermented with Bifidobacterium animalis subsp. lactis BB-12. Proximate composition and starch profiling showed significant differences among flours (p < 0.05), with GBF exhibiting the highest resistant starch (46.36 ± 0.94
Mislabeling of frozen thawed meat as fresh meat is a serious concern as the frozen thawed meat is having lesser consumer acceptance and inferior quality as compared to fresh meat. This research was done with the aim of development of a novel sandwich ELISA for the differentiation of fresh and frozen thawed pork meat, utilizing mitochondrial citrate synthase (CS) as a candidate biomarker enzyme. For the development of sandwich ELISA, polyclonal antibodies (pAb) were produced in two different laboratory animals (rabbits and guinea pigs) against the biomarker enzyme CS. The presence of anti-CS pAbs in the hyperimmune sera was confirmed by dot-blot analysis. A sandwich ELISA was optimized by utilizing rabbit anti-CS pAb as capture and guinea pig anti-CS pAb as detection antibody, both in 1:1000 dilution. The optimized sandwich ELISA attained a sensitivity and specificity of 91.43 % and 90.00 % respectively with an Area Under the Curve (AUC) of 0.953, at a cut-off value of 64.21 percentage positivity (PP). There was a significant difference (P < 0.05) observed between the PP values of fresh/chilled and frozen thawed pork meat. The limit of detection (LOD) and limit of quantification (LOQ) of the sandwich ELISA were calculated to be 3.71 ng/ml and 11.24 ng/ml, respectively. The sandwich ELISA was having 100.78 +/- 1.66 % of accuracy, and the assay was found to be having good repeatability as well as reproducibility. The assay showed a good storage stability up to 12 weeks of storage at refrigeration temperature (4 +/- 1 degrees C).
Chicken liver meat is a delicacy for consumers. The nutrient richness and unhygienic handling are responsible for deterioration of liver quality. To ensure the quality and freshness of chicken liver, an easy freshness detection technique is necessary. In this study, a dye-based pH-sensitive probe (PSP) was developed to monitor chicken liver freshness during its storage. The probe should not come in direct contact of the foods to be ingested was ensured, but all measurements were performed using a chicken liver slurry made solely for analytical purpose. At regular intervals, different quality parameters of stored chicken liver were assessed, and the freshness was checked with the developed PSP. Results showed that with the increasing storage intervals, the quality of the liver deteriorated significantly (p < 0.05), and at the point of spoilage, the PSP showed a visible color change in it. This color change of the probe was found to be well correlated with the acceptability of liver quality and its freshness. Therefore, the developed PSP was found to be an effective aid for monitoring the real-time freshness of stored chicken liver at different temperatures.
Poor valorization of buffalo hide is a financial loss to both farmers and the meat industries. Converting the hide into neutraceutical for diabetic patients will benefit diabetic patients, farmers and meat industry. Therefore, the objective of this study was to recover collagen hydrolysate (CH) from buffalo hide, characterize it and evaluate its antioxidant and antidiabetic activity. CH was extracted from buffalo hide using alcalase at different enzyme substrate ratios of 1:50, 1:100 and 1:200 (unit/w) and the corresponding CH samples thus obtained were referred as CH50, CH100 and CH200, respectively. One commercial collagen hydrolysate (CHM) was taken for comparison. The yield of CH200 (13.15%) was significantly (P<0.05) higher than CH50 and CH100. Degree of hydrolysis (DH) was significantly (P<0.05) higher for CH200 (25.60%) compared to other three CHs. Two protein bands of molecular weight lower than 11kDa were detected in CH50, CH100 and CH200. Antioxidant analysis revealed that the CH200 was better than CH50, CH100 and CHM. In-vitro antidiabetic activity showed that the dipeptidyl peptidase-IV (DPP-IV) inhibitory activity was significantly (P<0.05) higher (72.27%) for CH200 than CH50, CH100 and CHM at 5mg/mL concentration. The primary limitation of this study is its exclusive reliance on in-vitro assays which necessitates further validation. Our findings indicated that the one unit of alcalase per 200g of buffalo hide at 55 °C for 8h and pH 8 could be used to get better CH yield having higher DH, antioxidant and antidiabetic activity which might potentially serve as a natural antidiabetic neutraceutical.
The present study aimed to develop and characterize a functional goat milk-based nutritional supplement enriched with fermented finger millet and pearl millet, combining the nutritional benefits of goat milk with the enhanced bioactive potential of fermented millets. Goat milk was pasteurized and freeze-dried, while finger millet and pearl millet were fermented using Lactobacillus helveticus NCDC-292, dried, and milled. Lactic acid fermentation significantly enhanced the antioxidant potential of the millets, as evidenced by increased ABTS and DPPH radical scavenging activities. Pearl millet fermented with lactose for 48 h and finger millet fermented for 24 h exhibited the highest antioxidant activity and were selected for formulation. These millets, blended in equal proportions, were incorporated at varying levels (0–36
The study was conducted to isolate protein from chicken liver and characterization of its techno-functional properties. Prior to protein isolation, protein solubility test was carried out to know the highest solubility at a particular pH. The isolates obtained were freeze dried and subjected for different quality evaluation and comparison was made with the chicken liver powder. Higher protein solubility was observed at pH 1.5, 2.0 11.0 and 11.5 with significantly higher yield at alkaline pH and highest total protein content at pH 11.0. The bulk density of protein isolates was significantly lower than that of whole chicken liver powder. As compared to whole liver powder, the whiteness values were significantly higher for isolates and highest value was observed for isolate at pH 11.5 and accordingly had lowest total pigment content. The other techno-functional quality parameters such as fat absorption capacity, water absorption capacity, foaming capacity, foaming stability, emulsifying activity index, emulsifying stability index improved in all types of isolates. The ABTS and DPPH assays were also reflected significantly higher antioxidant activity in protein isolates as compared to whole liver powder. The protein isolates form poultry liver can be utilized for production of high-quality protein isolates.
The present study evaluated the storage stability of Lactobacillus helveticus (NCDC-292) fermented, freeze-dried chicken liver and heart protein hydrolysates. The resulting chicken liver hydrolysate powder (CLHP) and chicken heart hydrolysate powder (CHHP) were stored aerobically in PET jars at room temperature (27 ± 2°C) and analyzed over a 90-day period at 30-day intervals. Parameters assessed included pH, water activity, lipid oxidation, antioxidant activity, and microbial load. No significant changes in pH were observed throughout the storage period. However, water activity and TBARS values increased significantly (P < 0.05). Lipid oxidation remained within acceptable limits. Antioxidant activity, measured via DPPH and ABTS assays, declined significantly (P < 0.05) over time. A gradual increase in microbial counts was observed after the first 60 days, although the values remained within permissible limits. Overall, significant (P < 0.05) changes were observed in the quality attributes of both hydrolysates during aerobic storage. These findings highlight the necessity for enhanced packaging solutions to maintain the physicochemical and functional integrity of CLHP and CHHP, thereby supporting their potential use as functional food ingredients.
The meat and fish sectors are primary sources of animal protein for human consumption. However, they also generate large volumes of byproducts and organic waste annually, posing major challenges in terms of sustainable disposal. These byproducts have the potential to be repurposed into high-value, low-volume products, such as bioactive peptides or hydrolysates. Various methods used for the recovery of bioactive peptides from meat byproducts are enzymatic hydrolysis, microbial fermentation, ultrasonic-assisted, pulsed electric field, high hydrostatic pressure, microwave-assisted, and subcritical water processing. These bioactive peptides possess various functional properties, including antioxidant, antimicrobial, and antihypertensive effects. Incorporating them into food products could enhance both the functionality and quality of these products. In light of growing consumer demand for natural, eco-friendly ingredients, as well as sustainable practices in food production and packaging, the generation and use of bioactive peptides and hydrolysates offer a promising strategy. This approach not only mitigates environmental challenges but also fosters the sustainable growth of the meat and fishery industries, ensuring long-term ecological and economic viability. This review explores new opportunities and avenues for utilizing animal and marine byproducts in producing bioactive peptides and their potential applications in meat products and processing techniques, thereby supporting the sustainable growth of the meat and fishery industries.
A variation in storage temperature for meat products may occur accidentally and result in the spoilage of the products. The application of sensors to monitor temperature variation can ensure consumer safety by indicating food spoilage. In the present study, natural dye betalains were extracted from cockscomb flowers (Celosia argentea var. cristata) by using HCl-ethanol as a solvent and used to develop a temperature sensor (TS). The developed TS was attached to the aerobic packages of chicken meat patties and stored at different temperatures. At regular intervals, the changes in quality attributes of patties and the color of TS were assessed. Results showed that, with increasing time intervals, the TS could indicate temperature variation by changing its visible color. Different physicochemical, microbiological, and sensory quality attributes of patties and the instrumental color values of TS also changed (p<0.05) with the increasing time intervals at different temperatures. Interestingly, a similar pace of concurrence was observed between the quality changes in chicken patties and the changes in instrumental values and visible color of TS. Results showed the potency of betalains-based TS as an efficient temperature monitoring aid for the cold chain of chicken patties.
Globally, large quantity of animal byproducts is generated from the slaughter of food animals, but there is lack of research articles related to drying of these byproducts and its use as pet food. Therefore, this study was conducted with the aim of utilization of intact whole buffalo liver by drying for pet treat, evaluating its shelf life and palatability. The intact liver surface was superficially sliced, and the surface was pierced. Thereafter, the livers were pretreated in 3% sugar and 4% salt solution (1 : 3 w/v) for 3 h followed by microwaving for 4 min and hot air drying at 60 degrees C for 40 h (designated as T2L). The livers which were dried the same as T2L except surface piercing were referred as T1L, whereas the livers dried only using hot air oven were referred as control (CL). The moisture and protein contents of the dried CL and T2L were found to be 28.46% and 14.29% and 43.85% and 52.76%, respectively. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) image of T2L revealed the presence of few low as well as high molecular weight protein bands which were absent in CL and T1L indicating a comparatively lower level of protein degradation in T2L. The shelf life of T1L and T2L samples based on microbiological and lipid oxidation analyses was found to be more than 60 days at 25 and 4 degrees C. Palatability studies using dogs showed that all dried samples were highly palatable. Thus, it could be concluded that intact buffalo liver could be dried using surface slicing, with/without piercing followed by salt and sugar pretreatment, 4 min microwaving, and hot air drying at 60 degrees C for 40 h. Future study should focus on the sensory properties such as aroma, texture, and flavor and sensory analysis of the dried liver by human.
Study aimed to develop biomarker-based assay for rapid detection of fresh and frozen -thawed buffalo meat in the supply chain. The method is based on development of a solvent system and identification of suitable substrate and developer for screening of biomarkers. For the confirmation column chromatography, gel electrophoresis and Western Blotting were carried out. Validation was done by intra- and inter -day validation, storability study, and determination of thermal history. Best results were shown with pH 8.0 Tris-HCl; extraction buffer, 205 mu M nicotinamide adenine dinucleotide hydrogen; substrate, 184 mu M Nitroblue tetrazolium, and 1.9 mu M phenazine methosulfate; developer. The thermal history ranged from 0.14 to 0.17 during storage at -20 C-degrees. The intra- and inter -day assay precision (CV %) ranged from 5.3 to 6.5 %; in chilled and 14.1 - 9.2 % in frozen -thawed samples. The study confirmed SOD as a viable biomarker. Developed method using SOD has significant potential for rapidly differentiating chilled or frozen -thawed meat.
This study was conducted to characterize the extract collagen hydrolysate (CH) from low value buffalo skin using enzymes bromelain (B) and papain (P), including their bioactivities. Optimum levels of the two enzymes were determined by Sodium dodecyl sulphate-Polyacrylamide gel electrophoresis (SDS-PAGE) and degree of hydrolysis. Levels (30 and 50 units of B/g of skin and 20 and 30 units of P/g of skin) showing maximum degradation of collagen proteins were used to extract CH and the recovered CH were correspondingly referred as B20, B50, P20 and P30, respectively. The yield of CH from skin for P20, P30, B30 and B50 was 27.38, 26.32, 20.71 and 16.19
Aim of this study was to develop a rapid spectrometric method for monitoring chilled (CM) and frozen-thawed meat (FTM) in supply chain to find out the regulatory compliance. The method was developed with the standardization of extraction buffer, substrate and developer. SDS-PAGE clearly displayed presence of citrate synthase (CS) corresponding to MWt. of 42.5 KDa while Western blotting and ELISA data confirmed the presence of this enzyme. Validation data revealed very good precision of the method with coefficient of variation (CV, %) less than 10. To ascertain the thermal history, a threshold value (R1 value) less than 0.2 was established for samples subjected to freezing and thawing cycles, while meat samples exhibiting an R1 value of 0.9 or higher are classified as chilled meat which made clear demarcation in between the two types of meat. The CS enzyme showed very good stability on repeated freezing-thawing, and thus, CS has greater potential to acts a biomarker for distinguishing chilled and defrosted meat to meet the regulatory compliance.
Objective of this study was to optimize the processing conditions for preparation of chicken heart protein hydrolysates. Chicken heart protein hydrolysates were prepared by fermentation using L. helveticus and L. plantarum, and their concentrations and processing conditions were optimized according to pH, soluble protein content and degree of hydrolysis%. It was observed that there was significant (p
Gaddi goat milk whey protein fractions were hydrolysed using proteolytic enzyme-papain, and further subjected to in vitro digestion with gastric and intestinal digestion enzymes-pepsin, trypsin and pancreatin.Bioactive peptides obtained subsequently enzymatic hydrolysis and in vitro digested hydrolysates were centrifuged and supernatants exploited for characterization by SDS-PAGE, antioxidant, antihypertensive and antimicrobial activities.SDS-PAGE exhibited that Gaddi goat whey proteins degraded subsequently in vitro digestion of hydrolysates prepared with papain.OPA activity was noted highest (29.51 ± 0.18 mg/ml) in overnight in vitro digested Gaddi goat whey protein hydrolysates prepared with papain P1 (1:100) as compare to Gaddi goat whey protein digested hydrolysates prepared with papain P2 (0.01:100) and P3 (0.005:100).FRAP antioxidant values were noted higher (38.26 ± 0.06 mg/100ml) in Gaddi goat whey hydrolysates prepared with P1.DPPH antioxidant activity increases with time during enzymatic hydrolysis.DPPH antioxidant activity was observed higher (27.59 ± 0.53 %) after 4 h of enzymatic hydrolysis of Gaddi goat whey with P1.Dry dot TLC showed that DPPH activity remains stable afterwards overnight of spray in Gaddi goat whey hydrolysates prepared with varied concentration of papain.Antihypertensive activity was noted highest (72.70 ± 0.76 %) in overnight in vitro digested Gaddi goat whey protein hydrolysates prepared with P1.Antimicrobial activity was observed in digested samples of Gaddi goat whey protein hydrolysates generated with papain against Rhodococcus equi.Among the three concentrations of papain (P1, P2 and P3) used for the present study, antioxidant and antihypertensive activities were found highest in Gaddi goat whey protein hydrolysates prepared with enzyme-papain (P1), indicating likely application as bioactive and functional components in various food preparations.
Chicken is one of the most preferred protein sources for nonvegetarian consumers around the world. Due to the huge demand for quality chicken products, the processors and the suppliers need to maintain the optimum chicken quality during the supply chain. Therefore, this study was aimed to develop a suitable device to monitor chicken quality in supply chain. In the present study, a natural dye extracted from coleus blumei leaves ( Plectranthus scutellarioides ) has been used to develop a chicken quality monitoring sensor. This sensor has been tested for its color-changing ability by attaching inside the packet of fresh chicken at different storage temperatures viz., 4 ± 1, 10 ± 1, 15 ± 1, 25 ± 1, and 37 ± 1 °C. During the storage of chicken the changes in quality parameters (physicochemical, microbiological, and sensory attributes) were measured at regular intervals. The sensor showed a color change during the progress of the storage period and this was well in concurrence with the changes in the quality parameters of the chicken. The results showed the potentiality of the coleus blumei leaves dye-based sensor as a monitoring device to detect the quality of chicken during its storage at various temperatures.
The aim of the study was to investigate the effect of camel milk casein hydrolysates (CMCH) on physico-chemical, sensory, colour and textural quality characteristics of chevon patties. Camel milk casein was hydrolysed using three different proteolytic enzymes viz., alcalase (CMCH-A), αchymotrypsin (CMCH-C) and papain (CMCH-P). Four groups were prepared viz., CMCH: 0% (C), CMCH-A: 0.03% (T1), CMCH-C: 0.06% (T2) and CMCH-P: 0.09% (T3). The pH and emulsion stability of goat meat emulsions were comparable among the treatments. The pH, water activity and moisture of cooked chevon patties varied significantly (p<0.05) whereas cooking yield, protein, fat, ash and dietary fibre and dimensional characteristics (% gain in height and decrease in diameter) were comparable among treatments and control. Hardness, springiness, stringiness, cohesiveness, gumminess and resilience of chevon patties were significantly (p<0.05) different in treatments and control. Casein hydrolysate in chevon patties resulted in significant (p<0.05) increase in redness values, whereas lightness, yellowness and hue values decreased significantly (p<0.05) in treatment groups compared to control. Colour and appearance, texture and juiciness scores were significantly (p<0.05) different with higher values in treated products than control. The overall acceptability scores of C and T2 were also comparable and significantly (p<0.05) higher than T1 and T3. It was concluded that CMCH-C could be successfully incorporated in the formulation of chevon patties (@ 0.06%) withoutmuch effects onphysico-chemical,texturaland sensory attributes.