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Institution

National Dairy Research Institute

FacilityKarnāl, Himachal Pradesh, India
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.
Topics: Population, Sperm, Murrah buffalo, Gene, Semen


Papers
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Journal ArticleDOI
TL;DR: The relationship between the composition, texture and microstructure of chhana (an Indian-style soft cottage cheese analogue) and rasogolla (a sweetened dairy product made from chhanas) were analyzed in this paper.
Abstract: The relationships between the composition, texture and microstructure of chhana (an Indian-style soft cottage cheese analogue) and rasogolla (a sweetened dairy product made from chhana) were analysed. Chhana contained a significantly higher proportion of fat, protein, lactose and minerals than did rasogolla. Cooking of chhana in 60% sucrose solution introduced sucrose and changed the texture and structure to that typical of rasogolla. As chhana was transformed to rasogolla, the Instron textural properties, hardness, gumminess and chewiness, fell significantly, whereas springiness increased dramatically. Market rasogolla had a slightly different composition from the laboratory-made samples, but both had similar Instron textural and sensory textural attributes. Scanning electron microscopy showed that chhana had a structure like cottage cheese or cream cheese, a compact, coalesced casein matrix with fat globules embedded in it. Rasogolla had a conglomerated, ragged and porous casein matrix with uneven surface and numerous large void spaces. The collapsed and ruptured fat globules were found embedded in the agglomerated protein particles of rasogolla. The textural attributes of both chhana and rasogolla could be explained by the microstructure.

19 citations

Journal ArticleDOI
TL;DR: In this article, the results showed that despite the reduction in glucosinolate content by chemical treatment of mustard cake, its feeding as a sole protein source did not improve performance over untreated mustard cake.

19 citations

Journal ArticleDOI
TL;DR: The enzyme-linked aptamer-sorbent assay (ELASA) was evaluated as an assay of BCM-7 in biological fluids, and aptamer-coated gold nanoparticles (GNPs) resulted in color change of GNPs in the presence of BCm-7, thereby establishing recognition of BC M-7 by aptamers.
Abstract: β-Casomorphin-7 (BCM-7), a seven amino acid peptide, is released during digestion of β-casein A1 variant of milk which is speculated to be associated with certain diseases. Fifteen ssDNA aptamers having high affinity toward BCM-7 were identified from a 72 nt long random library after ten rounds of systematic evolution of ligands by exponential enrichment. Dissociation constant values of selected aptamers were in the range of 7.7–156.7 nM. Seq6 aptamer exhibited the lowest Kd value. Nine aptamers were evaluated for their binding toward BCM-7, BCM-9A1, and BCM-9A2 peptides, and binding was variable. SeqU5 exhibited the lowest binding with BCM-9A1 and BCM-9A2. Aptamer-coated gold nanoparticles (GNPs) resulted in color change of GNPs in the presence of BCM-7, thereby establishing recognition of BCM-7 by aptamers. The enzyme-linked aptamer-sorbent assay (ELASA) was evaluated as an assay of BCM-7 in biological fluids. BCM-7-peroxidase competed with BCM-7 in ELASA, performed with BCM-7 solution and BCM-7 spiked ...

19 citations

Journal ArticleDOI
TL;DR: In this paper, a method for the preparation of WPC-mineral (iron/zinc) complex was standardized on the basis of maximum mineral binding ability of proteins, and the method involving ultrafiltration and diafiltration (repeated washing to remove free mineral from retentate) has been standardized.
Abstract: Food fortification is the most cost effective, sustainable and optimal approach in the battle against iron and zinc deficiencies. Iron/zinc, being members of the transition metal series, are highly reactive and poses numerous challenges with respect to physicochemical stability of fortified foods. Whey proteins concentrate (WPC) produced as the principal byproduct of cheese or casein manufacturing is widely used as food ingredient. Among the various technologies explored, iron/zinc binding to milk proteins has long been understood and applied. Therefore, method for the preparation of WPC – mineral (iron/zinc) complex was standardized on the basis of maximum mineral binding ability of proteins. Method involving ultrafiltration and diafiltration (repeated washing to remove free mineral from retentate) has been standardized. Structural modification upon mineral binding was confirmed by RP-HPLC chromatograms. Both iron and zinc bound WPC complexes possessed good stability (resistance towards release of bound mineral) under different processing conditions. However, zinc bound WPC showed better heat stability and lower pH and ionic stability compared to iron bound WPC. The final protein – mineral complexes could be used as a suitable organic fortificants for various food applications with better solubility.

19 citations

Journal ArticleDOI
TL;DR: Low mean levels of oestrone sulphate were recorded in the non-pregnant and up to the fourth month of pregnancy with the levels rising sharply thereafter to a peak of 6559.82 pg/ml in the tenth month.

19 citations


Authors

Showing all 3289 results

NameH-indexPapersCitations
Vivek Sharma1503030136228
Rajesh Kumar1494439140830
Sanjay Kumar120205282620
Don C. Des Jarlais101657110906
Anil Kumar99212464825
Gaurav Sharma82124431482
Samuel R. Friedman7442722142
Ashwani Kumar6670318099
Ashutosh Sharma6657016100
Manoj Kumar6540816838
Tim Stockwell6038214797
Pankaj Gupta5760915251
Jyoti S. Choudhary4916313060
Bhupinder Singh474259643
Ashutosh Kumar452538751
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
202317
202284
2021325
2020265
2019191
2018223