National Dairy Research Institute

About: National Dairy Research Institute is a facility organization based out in Karnāl, Himachal Pradesh, India. It is known for research contribution in the topics: Population & Sperm. The organization has 3228 authors who have published 3524 publications receiving 51151 citations. The organization is also known as: Imperial Institute of Animal Husbandry and Dairying & Imperial Dairy Institute.

Preparation of spray-dried curcumin microcapsules using a blend of whey protein with maltodextrin and gum arabica and its in-vitro digestibility evaluation

Abstract: In the present study, attempts were made to prepare spray-dried curcumin microcapsules using a blend of whey proteins and carbohydrates. Curcumin was first dissolved in buffalo milk butteroil and then it was converted into an emulsion using skim milk, WPC-80, and a blend of maltodextrin and gum arabica as the wall material solids. Optimization of ingredients level for stable curcumin emulsion was done by varying core: wall material solids ratio and protein: carbohydrates ratio in the wall material solids. Particle size, zeta potential, viscosity, encapsulation efficiency, and emulsion stability of the emulsions were evaluated. Emulsion having core: wall material solids ratio of 1:2 and protein: carbohydrates ratio of 1:2 was found to yield stable emulsion with highest curcumin content and hence was selected for spray drying. Spray drying was performed at different inlet air temperatures. Bulk densities, encapsulation efficiency, moisture content, water activity, and reconstitution parameters decreased while DPPH free radical scavenging activity increased with an increase in the inlet air drying temperature. Inlet air temperature of 180 °C was found suitable for drying curcumin emulsion. In-vitro digestion of spray-dried curcumin microcapsules revealed that the developed encapsulate was resistant to gastric digestion but was digested by intestinal fluids.

Enzymatic hydrolysis of whey and its analysis

Abstract: An attempt was made to hydrolyze proteins and lactose in whey to improve the nutritive value of this byproduct, and extend its application as an ingredient to healthy beverages. Flavourzyme in different concentrations was used at pH 7.0 to hydrolyze protein at 50 °C. pH stat method, SDS-PAGE and RP HPLC–MS were used to evaluate degree of protein hydrolysis, pattern of peptide formation and characterize smaller peptides in hydrolysate, respectively. Higher concentration of enzymes produced more number of small peptides. Protein hydrolysate was again hydrolyzed at 30 °C with β—galactosidase at pH 5.5 to hydrolyze lactose. HPLC analysis indicated the degree of lactose hydrolysis and number of tri/poly saccharides formed due to varied enzyme concentration. Results from the experiment can be utilized to formulate healthy whey beverages for specific purpose.

Comparative oncology: Integrating human and veterinary medicine.

Abstract: Cancer constitutes the major health problem both in human and veterinary medicine. Comparative oncology as an integrative approach offers to learn more about naturally occurring cancers across different species. Canine models have many advantages as they experience spontaneous disease, have many genes similar to human genes, five to seven-fold accelerated ageing compared to humans, respond to treatments similarly as humans do and health care levels second only to humans. Also, the clinical trials in canines could generate more robust data, as their spontaneous nature mimics real-life situations and could be translated to humans.

In vitro evaluation of probiotic potential of Lactobacillus cultures of human origin capable of selenium bioaccumulation

Abstract: The probiotic potential of 5 food grade Lactobacillus strains, of human origin namely Lactobacillus fermentum (S23), Lb. fermentum NCDC77 (S8), Lb. fermentum (S25) and Lb. plantarum (S1), capable of selenium bioaccumulation (in previous studies), was investigated. The cultures, S8 and S23 maintained elevated cell numbers under conditions simulating passage through the human gastrointestinal tract, showing ability to survive in the presence of simulated gastric juice at pH 2. These cultures also survived in the presence of simulated intestinal juice with 1% bile salts. The cultures showed variable and strain dependent cell-surface hydrophobicity and auto-aggregation ability. The cultures were assayed for susceptibility to 20 antibiotics and found susceptible to 14 out of 20 antibiotics while showed variable resistance to remaining 6 antibiotics. S8 and S23 cultures showed superior antibacterial activity in comparison to remaining 3 cultures. These findings suggest that Lb. fermentum NCDC77 (S8) and Lb. fermentum (S23) cultures, endowed with the ability to accumulate high amount of selenium, exhibited high resistance against low pH and bile. Moreover, these cultures possessed adherence and auto-aggregation properties with minimum resistance to antibiotics and hence could be exploited for the development of selenium enriched functional food or nutraceutical as a source of dietary selenium.

Buffalo Cervico-Vaginal Fluid Proteomics with Special Reference to Estrous Cycle: Heat Shock Protein (HSP)-70 Appears to Be an Estrus Indicator

Abstract: Cervico-vaginal fluid (CVF) plays significant roles in coitus, sperm transport, and implantation. It is believed to be a good noninvasive biomarker for various diagnostic purposes. In this study, a comprehensive proteomic analysis of buffalo CVF was performed during the estrous cycle in order to document the protein expressions, utilizing SDS-PAGE, mass spectrometry, and immunoblot. The main objective was to screen the CVF of buffalo for one or more estrus-specific proteins. A total of 416 proteins were identified in the CVF of both estrus and diestrus phases. Out of these proteins, 68 estrus-specific proteins have been extensively reviewed in the protein database. The major physiological functions of estrus CVF proteins appeared to be stress response, immune response, and metabolic. Eventually, the expression level of heat shock protein-70 in the CVF during the estrus phase, as revealed in SDS-PAGE analysis, was higher than during diestrus. The identity of the protein was confirmed by immunoblot analysis as heat shock protein-70. The findings provide a potential lead for the evaluation of these proteins for estrus detection in buffalo because CVF biomarker detection is a noninvasive technique. The mass spectrometric data of identified proteins have been deposited at the ProteomeXchange with the identifier PXD000620.