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Relevant bibliographies by topics / Conarachin I

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Journal articles

Academic literature on the topic 'Conarachin I'

Author: Grafiati

Published: 5 June 2025

Last updated: 1 August 2025

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Journal articles on the topic "Conarachin I"

1

Zhang, Shaobing, Yushan Jiang, Shuyan Zhang, and Lin Chen. "Physical Properties of Peanut and Soy Protein-Based Emulsion Gels Induced by Various Coagulants." Gels 8, no. 2 (2022): 79. http://dx.doi.org/10.3390/gels8020079.

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Emulsions of peanut and soy proteins, including their major components (arachin, conarachin, glycinin and β−conglycinin), were prepared by ultrasonication (300 W, 20 min) at a constant protein concentration (4%, w/v) and oil fraction (30%, v/v). These emulsions were then induced by CaCl2, transglutaminase (TGase) and glucono-δ-lactone (GDL) to form emulsion gels. The optimum coagulant concentrations were obtained for peanut and soy protein-stabilized emulsion gels, such as CaCl2 (0.15 and 0.25 g/dL, respectively), TGase (25 U/mL) and GDL (0.3% and 0.5%, w/v, respectively). For the CaCl2-induce

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2

Sun, Qing Jie, Liu Xiong, Xiang Hui Bu, and Yan Liu. "Study on Mechanism of Cross-Linking of Peanut Protein Isolate Modified with Transglutaminase." Advanced Materials Research 550-553 (July 2012): 1304–8. http://dx.doi.org/10.4028/www.scientific.net/amr.550-553.1304.

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The mechanism of cross-linking of peanut protein isolate (PPI) modified with transglutaminase was investigated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier Transformation Infrared (FT-IR) spectra. SDS-PAGE banding patterns indicated that the contents of arachin and conarachin after transglutaminase (TGase) modification were decreased and high molecular weight polymers were formed. SDS-PAGE banding patterns also suggested that cross-linking effects were accomplished in the presence of transglutaminase and the main component participating in cross-linking

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3

Monteiro, P. Vincent, and V. Prakash. "Effect of proteases on arachin, conarachin I, and conarachin II from peanut (Arachis hypogaea L.)." Journal of Agricultural and Food Chemistry 42, no. 2 (1994): 268–73. http://dx.doi.org/10.1021/jf00038a008.

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4

Misra, J. B. "Variation in Nitrogen-to-Protein Conversion Factor for Peanut." Peanut Science 28, no. 2 (2001): 48–51. http://dx.doi.org/10.3146/i0095-3679-28-2-2.

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Abstract For peanut, a factor of 5.46 is used for converting nitrogen concentration into protein concentration because the peanut proteins arachin and conarachin contain 18.31% nitrogen. Using published reports on the amino acid composition of peanut genotypes, the nitrogen-to-protein conversion factors (NPCF) for arachin and conarachin, as well as for whole peanut kernel were calculated. The value of NPCF for arachin varied between 5.271 and 5.563 and that for conarachin from 5.076 to 5.496. The location of crop growth may significantly affect the value of NPCF for whole kernels. For the samp

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5

Sumanta, Kumar Ghatak, Chattopadhyay Pabitra, and Sen Kamalika. "Molecular interaction of peanut proteins with some bio-pesticides: A comparative spectral study." Journal of Indian Chemical Society Vol. 97, No. 12a, Dec 2020 (2020): 2593–600. https://doi.org/10.5281/zenodo.5655906.

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Department of Chemistry, The University of Burdwan, Golapbag, Burdwan-713 104, West Bengal, India Department of Chemistry, University of Calcutta, 92, Acharya Prafulla Chandra Road, Kolkata-700 009, India <em>E-mail: </em>kamalchem.roy@gmail.com <em>Manuscript received online 15 November 2020, revised and accepted 25 December 2020</em> Safety and quality of food supplies is an essential part of consumer protection. Due to proven toxicity of synthetic pesticides, bio-pesticides are slowly capturing the agro-economy. It is now time to evaluate the different aspects of bio-pesticides that might h

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6

Sumanta, Kumar Ghatak, Majumdar Dipanwita, Singha Achintya, and Sen Kamalika. "Peanut proteins in selective sensing of BiIII at trace concentrations." Journal of Indian Chemical Society Vol. 94, Jul 2017 (2017): 773–80. https://doi.org/10.5281/zenodo.5606420.

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Department of Chemistry, University of Calcutta, 92, Acharya Prafulla Chandra Road, Kolkata-700 009, India <em>E-mail</em> : kamalchem.roy@gmail.com Department of Physics, Bose Institute, 93/1, Acharya Prafulla Chandra Road, Kolkata-700 009, India <em>Manuscript received 20 April 2017, accepted 08 May 2017</em> Bismuth is an environmentally significant element due to its usefulness in different aspects of life especially in semiconductors, cosmetics and pharmaceutical industries. It is less soluble in aqueous medium so it is poorly absorbed in human cells, however it plays a crucial role in va

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7

CHIOU, ROBIN Y. Y. "EFFECTS OF HEAT TREATMENTS ON PEANUT ARACHIN AND CONARACHIN." Journal of Food Biochemistry 14, no. 3 (1990): 219–32. http://dx.doi.org/10.1111/j.1745-4514.1990.tb00835.x.

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8

Sumanta, Kumar Ghatak, and Sen Kamalika. "Biodistribution of iron and zinc in peanuts: Analysis of biomolecular fractions." Journal of India Chemical Society Vol. 95, Apr 2018 (2018): 453–58. https://doi.org/10.5281/zenodo.5642592.

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Department of Chemistry, The University of Burdwan, Burdwan-713 104, West Bengal, India Department of Chemistry, University of Calcutta, 92, Acharya Prafulla Chandra Road, Kolkata-700 009, India E-mail: kamalchem.roy@gmail.com <em>Manuscript received 01 February 2018, revised 27 February 2018, accepted 28 February 2018</em> Peanuts are good source of plant proteins for human beings. Peanuts are also rich in iron and zinc. Iron is one of the essential macro elements for human body, whereas zinc is an essential micro element for brain development and enzymatic actions. In this work peanut protei

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9

Shetty, K. Jayarama, and M. S. Narasinga Rao. "STUDIES ON GROUNDNUT PROTEINS. VI. ISOLATION, CHARACTERISATION AND HYDROGEN ION TITRATION OF CONARACHIN II." International Journal of Peptide and Protein Research 9, no. 1 (2009): 11–17. http://dx.doi.org/10.1111/j.1399-3011.1977.tb01832.x.

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10

Li, Hua-Guang, Lei Wang, Yi-Shun Zhang та ін. "Cloning and sequencing of the gene Ahy-β encoding a subunit of peanut conarachin". Plant Science 168, № 6 (2005): 1387–92. http://dx.doi.org/10.1016/j.plantsci.2004.09.028.

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