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Journal articles on the topic 'Conarachin I'

Author: Grafiati

Published: 5 June 2025

Last updated: 1 August 2025

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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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11

Yu, Lina, Jie Sun, Shaofang Liu, Jie Bi, Chushu Zhang, and Qingli Yang. "Ultrasonic-Assisted Enzymolysis to Improve the Antioxidant Activities of Peanut (Arachin conarachin L.) Antioxidant Hydrolysate." International Journal of Molecular Sciences 13, no. 7 (2012): 9051–68. http://dx.doi.org/10.3390/ijms13079051.

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12

Hu, Xiao, Ziqi He, Peiying He, and Min Wang. "Microfluidization treatment improve the functional and physicochemical properties of transglutaminase cross-linked groundnut arachin and conarachin." Food Hydrocolloids 130 (September 2022): 107723. http://dx.doi.org/10.1016/j.foodhyd.2022.107723.

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13

Sun, Xiaoyang, Wen Zhang, Lifen Zhang, Shaojun Tian, and Fusheng Chen. "Molecular and emulsifying properties of arachin and conarachin of peanut protein isolate from ultrasound-assisted extraction." LWT 132 (October 2020): 109790. http://dx.doi.org/10.1016/j.lwt.2020.109790.

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14

Feng, Xiao-Long, Hong-Zhi Liu, Ai-Min Shi, Li Liu, Qiang Wang, and Benu Adhikari. "Effects of transglutaminase catalyzed crosslinking on physicochemical characteristics of arachin and conarachin-rich peanut protein fractions." Food Research International 62 (August 2014): 84–90. http://dx.doi.org/10.1016/j.foodres.2014.02.022.

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15

Yu, Lina, Weiqiang Yang, Jie Sun, Chushu Zhang, Jie Bi, and Qingli Yang. "Preparation, characterisation and physicochemical properties of the phosphate modified peanut protein obtained from Arachin Conarachin L." Food Chemistry 170 (March 2015): 169–79. http://dx.doi.org/10.1016/j.foodchem.2014.08.047.

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16

Qiu, Chaoying, Xiao Hu, Laihao Li, Xianqing Yang, Mouming Zhao, and Jiaoyan Ren. "Effect of transglutaminase cross-linking on the conformational and emulsifying properties of peanut arachin and conarachin fractions." European Food Research and Technology 243, no. 6 (2016): 913–20. http://dx.doi.org/10.1007/s00217-016-2804-z.

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17

Mills, E. N. C., J. Jenkins, N. Marigheto, P. S. Belton, A. P. Gunning, and V. J. Morris. "Allergens of the cupin superfamily." Biochemical Society Transactions 30, no. 6 (2002): 925–29. http://dx.doi.org/10.1042/bst0300925.

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The cupin family comprises a family of proteins possessing a common β-barrel structure that is thought to have originated in a prokaryotic ancestor. This structural motif is found as a single domain in fungal spherulins, fern sporulins and the germins/oxalate oxidase proteins of plants, while the globular storage proteins of plants, called legumins (11 S) and euvicilins (7 S), are two-domain cupins. The 11 S globulins are hexameric heteroligomeric proteins of Mr ~ 360000, with each subunit comprising an acidic 30000–40000-Mr polypeptide that is disulphide-linked to a 20000-Mr basic polypeptide

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18

Hu, Xiao, William Kwame Amakye, Peiying He, Min Wang, and Jiaoyan Ren. "Effects of microfluidization and transglutaminase cross-linking on the conformations and functional properties of arachin and conarachin in peanut." LWT 146 (July 2021): 111438. http://dx.doi.org/10.1016/j.lwt.2021.111438.

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19

Yu, Li Na, Qing Li Yang, Jian Xiong Feng, Jie Sun, Jie Bi, and Chu Shu Zhang. "Preparation and Antioxidant Activities of Peanut (Arachin conarachin L.) Protein Peptides by Lactobacillus Solid State Fermentation Method." Applied Mechanics and Materials 668-669 (October 2014): 1573–76. http://dx.doi.org/10.4028/www.scientific.net/amm.668-669.1573.

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The objective of this work is to study on the preparation of peanut protein peptide by lactobacillus solid state fermentation method and to provide a theoretical basis for further investigating peanut meal special protein material product. Results indicated that the soluble nitrogen concentration of peanut protein peptide could reach 70.92mg/ml, 1, 1-diphenyl-2-picryl-hydrazyl (DPPH) and hydroxyl free radicals scavenging rates were 95.00% and 86.28%, respectively, under the following optimum conditions: addition of nutrient salt solution volume of 25ml, lactobacillus liquid volume of 5ml, temp

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20

Yu, Li Na, Jian Xiong Feng, Qiang Qiang Ming, et al. "Preparation and Antioxidant Activities of Peanut (Arachin conarachin L.) Protein Peptides by Bacillus Subtilis Solid State Fermentation Method." Advanced Materials Research 887-888 (February 2014): 601–4. http://dx.doi.org/10.4028/www.scientific.net/amr.887-888.601.

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The objective of this work is to study on preparation of peanut protein peptide by bacillus subtilis solid state fermentation method. Results indicated that soluble nitrogen concentration of protein peptide could reach 122.86mg/mL, 1, 1-diphenyl-2-picryl-hydrazyl (DPPH) and hydroxyl free radicals scavenging rates were 85.22% and 84.88%, respectively, under the following optimum conditions: nutrient salt solution of 16.3mL, bacterial suspension volume of 3.8mL, temperature of 45°C, and time of 41h. IC50values for scavenging of DPPH, hydroxyl and superoxide anion free radicals rates, iron and co

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21

Rezende, Jaqueline de Paula, Hauster Maximiler Campos De Paula, Talma Duarte Freitas, Yara Luiza Coelho, Luis Henrique Mendes Da Silva, and Ana Clarissa dos Santos Pires. "Application of Congo red dye as a molecular probe to investigate the kinetics and thermodynamics of the formation processes of arachin and conarachin nanocomplexes." Food Chemistry 384 (August 2022): 132485. http://dx.doi.org/10.1016/j.foodchem.2022.132485.

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22

Chen, Chen, Yan Du, and Fusheng Chen. "Effect of urea concentration on properties of peanut protein isolate, arachin and conarachin-based adhesives during urea-epichlorohydrin modification." Royal Society Open Science 8, no. 3 (2021). http://dx.doi.org/10.1098/rsos.202227.

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To lay a theoretical basis for the preparation of peanut protein-based adhesives and promote the sustainable development of the adhesive industry, properties of peanut protein isolate (PPI), arachin and conarachin-based adhesives modified by urea and epichlorohydrin (ECH) were investigated under different urea concentrations. When the urea concentration was 2 mol l −1 , the wet shear strength of the PPI-based adhesive was 1.24 MPa with the best water resistance. With the increase of urea concentration from 0 to 4 mol l −1 , the apparent viscosity of the PPI-based adhesive increased from 3.87 t

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23

Jiang, Shan, Junting Zhang, Suhong Li, and Chunhong Zhang. "Effect of enzymatic hydrolysis on the formation and structural properties of peanut protein gels." International Journal of Food Engineering, November 20, 2020. http://dx.doi.org/10.1515/ijfe-2018-0356.

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AbstractThe limited enzymatic hydrolysis gelation method was investigated using peanut protein isolate (PPI) without any coagulators. A peanut protein gel could be formed by enzyme treatment with Alcalase at low temperature (50–70 °C). The influence of enzymatic hydrolysis on the rheological and physicochemical properties was investigated. Structural changes in the PPI were characterized by analyzing the subunits, chemical forces, surface hydrophobicity, fluorescence spectra, and circular dichroism (CD) spectra. The results revealed that enzymatic hydrolysis significantly affected the conarach

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24

SUVENDU MONDAL and ANAND M BADIGANNAVAR. "Development of high protein groundnut (Arachis hypogaea L.) mutant through induced mutagenesis." Journal of Oilseeds Research 33, no. 2 (2023). http://dx.doi.org/10.56739/jor.v33i2.138886.

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Groundnut is used as a food crop for its oil, protein content and other valuable bioactive compounds. Inducedmutagenesis played an important role to generate genetic variability in this crop. Here we report the identificationof a high protein mutant from a mutagenized population of a rust resistant breeding line, TG 66. The mutant, TGM206 revealed a 19.8 per cent increment of seed protein content compared to its parent. Through protein analysis itwas found that the conarachin fraction was selectively increased in this mutant.

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25

Li, Wenjun, Chao Zhang, Ning Xu, et al. "Effect of lipoxygenase‐induced oxidation on molecular structure and digestive properties of arachin and conarachin." Journal of Food Processing and Preservation, August 23, 2021. http://dx.doi.org/10.1111/jfpp.15874.

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26

Yang, Qin, Ya-Ru Wang, Ya-Nan Du, and Han-Qing Chen. "Comparison of the assembly behavior and structural characteristics of arachin and conarachin amyloid-like fibrils." Food Hydrocolloids, January 2023, 108479. http://dx.doi.org/10.1016/j.foodhyd.2023.108479.

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