University of Calcutta (informally known as Calcutta University or CU) is a collegiate public state university located in Kolkata, West Bengal, India.&nbsp;Within India it is recognized as a &quot;Five-Star University&quot; and accredited &quot;A&quot; Grade by National Assessment and Accreditation Council.

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The University of Calcutta has secured the Fifth position among the Universities of India in the prestigious &quot;Indian University Ranking 2019&quot; list, released by the NIRF of the Ministry of Human Resource Development, Government of India.

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It was established on 24 January 1857, and was one of the first institutions in Asia to be established as a multidisciplinary and Western-style university. Its alumni and faculty include several heads of state, heads of government, social reformers, prominent artists, only academy award winner and Dirac medal winner in India, many Fellows of the Royal Society and five Nobel laureates as of 2019 which is highest in South Asia.

University Of Calcutta

Para-coumaric acid (p-CA) is a plant derived secondary metabolite belonging to the phenolic compounds. It is widely distributed in the plant kingdom and found mainly in fruits, vegetables, and cereals. Various in vivo and in vitro studies have revealed its scavenging and antioxidative properties in the reduction of oxidative stress and inflammatory reactions. This evidence-based review focuses on the protective role of p-CA including its therapeutic potential. p-CA and its conjugates possesses various bioactivities such as antioxidant, anti-inflammatory, anti-cancer, anti-diabetic, and anti-melanogenic properties. Due to its potent free radical scavenging activity, it can mitigate the ill effects of various diseases including arthritis, neurological disorders, and cardio-vascular diseases. Recent studies have revealed that p-CA can ameliorate the harmful effects associated with oxidative stress in the reproductive system, also by inhibiting enzymes linked with erectile function. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

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Botany

Fulltext

Antioxidants

Scavenging properties of plant-derived natural biomolecule para-coumaric acid in the prevention of oxidative stress-induced diseases

DNA was isolated from 14 cultivars of Vigna radiata (L.) Wilczek and subjected to RAPD analysis using 14 random decamer primers. These cultivars revealed polymorphism with respect to RAPD markers and were subjected to hierarchical cluster analysis. A dendrogram was prepared based on these data. Analysis of banding patterns confirmed that two strongly aromatic cultivars IC1, IC4, were closely linked. But another aromatic cultivar, B1, formed a separate cluster. The high yielding cultivars were closely related to B1. The phylogenetic tree constructed by the neighbour joining method showed that RAPD results were correlated with morphological characters like plant height, leaf and seed size, seed colour, etc.

GENERAL

Bio-Physics, Molecular Biology and Bioinformatics

Biologia Plantarum

Estimation of genetic variability of Vigna radiata cultivars by RAPD analysis

A number of trypsin inhibitor (TI) genes have been used to generate insect-resistant plants. Here we report a novel trypsin inhibitor from Indian mustard Brassica juncea (BjTI) that is unique in being the precursor of a 2S seed storage protein. The inhibitory activity is lost upon processing. The predicted amino acid sequence of the precursor based on the B. juncea 2S albumin (Bj2S) gene cloned and sequenced in this laboratory (Bj2Sc; GenBank™ accession number X65972) showed a soy-bean-TI active site-like motif GPFRI at the expected processing site. The BjTI was found to be a thermostable Kunitz type TI that inhibits trypsin at a molar ratio of 1:1. The 20-kDa BjTI was purified from midmature seeds and found to be processed in vitro to 9- and 4-kDa subunits upon incubation with seed extract. The Bj2Sc sequence was expressed in Escherichia coli pET systems as the inhibitor precursor. The radiolabeled gene product was expressed in vitro in a coupled transcription-translation system and showed the expected processing into subunits. Two in vitro expressed pre-2S proteins, mutated at Gly and Asp residues, were processed normally to mature subunits, showing thereby no absolute requirement of Gly and Asp residues for processing. Finally, the 2S gene was introduced into tobacco and tomato plants. Third generation transgenics expressing BjTI at 0.28-0.83% of soluble leaf proteins showed remarkable resistance against the tobacco cutworm, Spodoptera litura. This novel TI can be used in transforming seed crops for protection to their vegetative parts and early seed stages, when insect damage is maximal; as the seeds mature, the TI will be naturally processed to the inactive storage protein that is safe for consumption.

Journal of Biological Chemistry

Precursor of the inactive 2S seed storage protein from the Indian mustard Brassica juncea is a novel trypsin inhibitor. Characterization, post-translational processing studies, and transgenic expression to develop insect-resistant plants

Although dielectric relaxation can significantly affect the intrinsic fluorescence properties of a protein, usually it is fast compared to fluorescence timescales and needs to be slowed down by adding viscogens or lowering temperature before its impact on fluorescence can be studied. We report here a remarkable blue shift in fluorescence upon bimolecular quenching in the single-tryptophan thermostable protein Bj2S, the 2S seed albumin from Brassica juncea, at ambient temperature and viscosity. The magnitude of the blue shift (∼5 nm at 50% quenching by acrylamide) is striking in a single-tryptophan protein and is attributed to a slowly relaxing dielectric environment in Bj2S from red edge excitation, steady-state polarization and time-resolved fluorescence experiments. Our results have important implications on interpretation of fluorescence of proteins with highly constrained backbones and in designing model systems for studying slow protein solvation dynamics using Trp fluorescence as the reporter probe. © 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

FEBS Letters

Dielectric relaxation in a single tryptophan protein

Seed storage proteins of grain crops meet the major dietary protein requirement of over half of the world population. However, seed proteins in general are deficient in some essential amino acids and hence are of poor nutritional quality. Therefore, intensive research is going on to isolate and characterize these proteins and their genes, and to produce transgenic crop plants with modified seed protein genes, with a view to improving their nutritive value as human food and animal feed. Many seed storage protein genes from cereals, legumes and oil seeds have been isolated, sequenced and their regulation has been studied by promoter deletion assay in transgenic plants. The amino acid composition of seed proteins of some transgenic crops has been marginally improved by modifying these genes for more methionine and lysine codons by site-directed mutagenesis or by introducing heterologous genes. The synthesis, processing and targeting of the introduced gene products and their stable expression in successive generations of transgenic plants have also been studied. The potentiality of such genetic engineering approaches has been amply demonstrated. But problems of control over copy number and site of integration of the foreign gene and the position effect of the changes in the amino acid in the polypeptide chain on the final level of expression and deposition of the correctly processed storage protein remains unsolved. More basic research is needed before large-scale application of this approach for improvement of nutritional quality of seed proteins becomes possible.