Výsledky vyhledávání - "Dipak K. Bhattacharyya"

Improvement of β-galactosidase production by solid-state fermentation using cauliflower (Brassica oleraceae var. botrytis) waste by Enterobacter aerogenes KCTC2190

Autor: Manisha Maity, Dipak K. Bhattacharyya, Jayati Bhowal

Publikováno v: Research Journal of Biotechnology. 18:18-23

In this present study, cauliflower wastes were employed as a substrate for better β-galactosidase production by Enterobacter aerogenes KCTC2190. Cauliflower leaf and stalk were used separately as substrates for solid state fermentation. 10% cauliflo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a150a4579a42fbe0a3e3a7033075d4a5
https://doi.org/10.25303/1803rjbt18023

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Evaluation of Prebiotic Properties of Galactooligosaccharides Produced by Transgalactosylation Using Partially Purified β-Galactosidase from Enterobacter aerogenes KCTC2190

Autor: Manisha Maity, Sayari Majumdar, Dipak K. Bhattacharyya, Jayati Bhowal, Ankita Das, Ananya Barui

Publikováno v: Applied Biochemistry and Biotechnology. 195:2294-2316

Transgalactosylation reaction is the penultimate step in the production of galactooligosaccharides (GOSs) which has prominent applications in the treatment of disorders. In the present study, partially purified β-galactosidase from Enterobacter aero

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::803ff800b05f4a6be3d735aacf4c7625
https://doi.org/10.1007/s12010-022-04073-6

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Effect of Fungal Fermentation on Enhancement of Nutritional Value and Antioxidant Activity of Defatted Oilseed Meals

Autor: Ruma Dutta, Saheli Ghosal, Dipak K. Bhattacharyya, Jayati Bhowal

Publikováno v: Applied biochemistry and biotechnology.

Agro-industrial residues contain high nutritive value. Nowadays, various advanced researches have been done for the production of various value-added products, using these wastes as substrates in the fermentation media. Flaxseed, mustard, and rice br

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ef84cc312cdca528e8f34ddc5f3954a
https://pubmed.ncbi.nlm.nih.gov/35819688

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Differential Localization of Protein Kinase C δ by Phorbol Esters and Related Compounds Using a Fusion Protein with Green Fluorescent Protein

Autor: Peter M. Blumberg, Dipak K. Bhattacharyya, Susan H. Garfield, Kassoum Nacro, Victor E. Marquez, Qiming J. Wang

Publikováno v: Journal of Biological Chemistry. 274:37233-37239

Enzyme localization often plays a controlling role in determining its activity and specificity. Protein kinase C (PKC) has long been known to translocate in response to physiological stimuli as well as to exogenous ligands such as the phorbol esters.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b5502469e268f144b06911ff714f3ac
https://doi.org/10.1074/jbc.274.52.37233

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Vitamin K2 (menaquinone) biosynthesis in Escherichia coli: evidence for the presence of an essential histidine residue in o-succinylbenzoyl coenzyme A synthetase

Autor: Dipak K. Bhattacharyya, R. Meganathan, O. Kwon

Publikováno v: Journal of Bacteriology. 179:6061-6065

o-Succinylbenzoyl coenzyme A (OSB-CoA) synthetase, when treated with diethylpyrocarbonate (DEP), showed a time-dependent loss of enzyme activity. The inactivation follows pseudo-first-order kinetics with a second-order rate constant of 9.2 x 10(-4) +

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0f717ddb56d235e23e29ea5c0212179
https://doi.org/10.1128/jb.179.19.6061-6065.1997

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Involvement of Arginine 120, Glutamate 524, and Tyrosine 355 in the Binding of Arachidonate and 2-Phenylpropionic Acid Inhibitors to the Cyclooxygenase Active Site of Ovine Prostaglandin Endoperoxide H Synthase-1

Autor: William L. Smith, Caroline Jill Rieke, Marc Lecomte, R. Michael Garavito, Dipak K. Bhattacharyya

Publikováno v: Journal of Biological Chemistry. 271:2179-2184

Examination of the crystal structure of the ovine prostaglandin endoperoxide synthase-1 (PGHS-1)/S- flurbiprofen complex (Picot, D., Loll, P.J., and Garavito, R.M. (1994) Nature 367, 243-2491) suggests (a) that the carboxyl group of arachidonic acid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::634084b055adf7eba4888c6c27b36f3e
https://doi.org/10.1074/jbc.271.4.2179

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Conformationally constrained analogues of diacylglycerol (DAG). 16. How much structural complexity is necessary for recognition and high binding affinity to protein kinase C?

Autor: Nancy E. Lewin, Samira Benzaria, Jeewoo Lee, Victor E. Marquez, Dipak K. Bhattacharyya, Kassoum Nacro, Peter M. Blumberg, Ji-Hye Kang, Kee-Chung Han, Bruno Bienfait

Publikováno v: Journal of medicinal chemistry. 43(5)

The design of potent protein kinase C (PK-C) ligands with low nanomolar binding affinities was accomplished by the combined use of pharmacophore- and receptor-guided approaches based on the structure of the physiological enzyme activator, diacylglyce

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39fd64cb05a5615ab7971428431b3a59
https://pubmed.ncbi.nlm.nih.gov/10715158

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