From Wikipedia, the free encyclopedia

Napin is one of the two most abundant seed storage proteins in the seeds of dicot crop mustard and rapeseed ( Brassica napus L., B. juncea L. Czern., B. nigra L. W.D.J.Koch, B. rapa L. and Sinapis alba L.). [1] [2] They are water soluble low-molecular weight basic proteins classified as 2S or 1.7S proteins, representing 20–40% of total seed protein, and having a molecular weight in the range of 12–17 kDa. [3] [4] Their isoelectric point varies based on the method of extraction and the specific characteristics of the isoforms that exist. They are composed of two polypeptide chains, a 4.5 kDa small subunit and a large 10 kDa subunit, stabilized primarily by disulphide bonds. Their secondary structure shows a high α-helical content. [5]

Properties

Arginine, lysine, and cysteine make napines excellent antibacterials, and since it's a basic protein, it can change its acidity to make it more effective. [6] Some in silico and in vitro antimicrobial activity screening reported napins as antimicrobial [5] [7] [2] and antifungal peptides. [8] [9]

Structure

As a basic protein, napin can be used to bind together and determine the shape, properties, and be able to synthesize when seeds develop. [10]

Composition

In terms of molecular weights, napin polypeptide chains are made up of 9,900 and 4,000 amino acids held together by disulfide bonds .The amino acid sequence of napin cDNA clones and napin peptide fragments indicate napin starts as a 178-residue precursor. [10]

Solubility

Napin is water soluble and soluble in a wide pH range. [11]

References

  1. ^ Rahman, M. (2018). "Brassicaceae mustards: Traditional and agronomic uses in Australia and New Zealand". Molecules. 23 (1): 231. doi: 10.3390/molecules23010231. PMC  6017612. PMID  29361740.
  2. ^ a b Rahman, M. (2020). Identification, Molecular and Proteomic Characterisation of Brassica rapa Seed Storage Proteins with Allergenic and Antimicrobial Potential (Thesis). Southern Cross University, Australia.
  3. ^ Rahman, M. (2000). "In Silico, Molecular Docking and In Vitro Antimicrobial Activity of the Major Rapeseed Seed Storage Proteins". Frontiers in Pharmacology. 11: 1340. doi: 10.3389/fphar.2020.01340. PMC  7508056. PMID  33013372.  This article incorporates text available under the CC BY 4.0 license.
  4. ^ Rahman, M. (2000). "Identification, characterization and epitope mapping of proteins encoded by putative allergenic napin genes from Brassica rapa". Clinical and Experimental Allergy. 50 (7): 848–868. doi: 10.1111/cea.13612. PMID  32306538. S2CID  216029445.
  5. ^ a b Rahman, M. (2000). "In Silico, Molecular Docking and In Vitro Antimicrobial Activity of the Major Rapeseed Seed Storage Proteins". Frontiers in Pharmacology. 11: 1340. doi: 10.3389/fphar.2020.01340. PMC  7508056. PMID  33013372.
  6. ^ Cheung, LamLam (December 2013). The Emulsifying Properties of Cruciferin Rich and Napin Rich Protein Isolates From Brassica Napus L (Master of Science thesis). University of Saskatchewan. CiteSeerx10.1.1.848.5181.
  7. ^ Munir, A. (2000). "In silico studies and functional characterization of a napin protein from seeds of Brassica juncea" (PDF). International Journal of Agriculture and Biology. 19–1092. doi: 10.17957/IJAB/15.1247 (inactive 31 January 2024).{{ cite journal}}: CS1 maint: DOI inactive as of January 2024 ( link)
  8. ^ Mignone, G. (2022). "Isolation of the mustard Napin protein Allergen Sin a 1 and characterisation of its antifungal activity". Biochemistry and Biophysics Reports. 29 (101208): 101208. doi: 10.1016/j.bbrep.2022.101208. PMC  8777239. PMID  35079640.
  9. ^ Jyothi, T. C. (2007). "Napin from Brassica juncea: Thermodynamic and structural analysis of stability". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1774 (7): 907–919. doi: 10.1016/j.bbapap.2007.04.008. PMID  17544981.
  10. ^ a b Ericson, M. L.; Rödin, J.; Lenman, M.; Glimelius, K.; Josefsson, L. G.; Rask, L. (1986-11-05). "Structure of the rapeseed 1.7 S storage protein, napin, and its precursor". The Journal of Biological Chemistry. 261 (31): 14576–14581. doi: 10.1016/S0021-9258(18)66909-1. ISSN  0021-9258. PMID  3771543.
  11. ^ Perera, Suneru P.; McIntosh, Tara C.; Wanasundara, Janitha P. D. (2016-09-07). "Structural Properties of Cruciferin and Napin of Brassica napus (Canola) Show Distinct Responses to Changes in pH and Temperature". Plants. 5 (3): E36. doi: 10.3390/plants5030036. ISSN  2223-7747. PMC  5039744. PMID  27618118.


From Wikipedia, the free encyclopedia

Napin is one of the two most abundant seed storage proteins in the seeds of dicot crop mustard and rapeseed ( Brassica napus L., B. juncea L. Czern., B. nigra L. W.D.J.Koch, B. rapa L. and Sinapis alba L.). [1] [2] They are water soluble low-molecular weight basic proteins classified as 2S or 1.7S proteins, representing 20–40% of total seed protein, and having a molecular weight in the range of 12–17 kDa. [3] [4] Their isoelectric point varies based on the method of extraction and the specific characteristics of the isoforms that exist. They are composed of two polypeptide chains, a 4.5 kDa small subunit and a large 10 kDa subunit, stabilized primarily by disulphide bonds. Their secondary structure shows a high α-helical content. [5]

Properties

Arginine, lysine, and cysteine make napines excellent antibacterials, and since it's a basic protein, it can change its acidity to make it more effective. [6] Some in silico and in vitro antimicrobial activity screening reported napins as antimicrobial [5] [7] [2] and antifungal peptides. [8] [9]

Structure

As a basic protein, napin can be used to bind together and determine the shape, properties, and be able to synthesize when seeds develop. [10]

Composition

In terms of molecular weights, napin polypeptide chains are made up of 9,900 and 4,000 amino acids held together by disulfide bonds .The amino acid sequence of napin cDNA clones and napin peptide fragments indicate napin starts as a 178-residue precursor. [10]

Solubility

Napin is water soluble and soluble in a wide pH range. [11]

References

  1. ^ Rahman, M. (2018). "Brassicaceae mustards: Traditional and agronomic uses in Australia and New Zealand". Molecules. 23 (1): 231. doi: 10.3390/molecules23010231. PMC  6017612. PMID  29361740.
  2. ^ a b Rahman, M. (2020). Identification, Molecular and Proteomic Characterisation of Brassica rapa Seed Storage Proteins with Allergenic and Antimicrobial Potential (Thesis). Southern Cross University, Australia.
  3. ^ Rahman, M. (2000). "In Silico, Molecular Docking and In Vitro Antimicrobial Activity of the Major Rapeseed Seed Storage Proteins". Frontiers in Pharmacology. 11: 1340. doi: 10.3389/fphar.2020.01340. PMC  7508056. PMID  33013372.  This article incorporates text available under the CC BY 4.0 license.
  4. ^ Rahman, M. (2000). "Identification, characterization and epitope mapping of proteins encoded by putative allergenic napin genes from Brassica rapa". Clinical and Experimental Allergy. 50 (7): 848–868. doi: 10.1111/cea.13612. PMID  32306538. S2CID  216029445.
  5. ^ a b Rahman, M. (2000). "In Silico, Molecular Docking and In Vitro Antimicrobial Activity of the Major Rapeseed Seed Storage Proteins". Frontiers in Pharmacology. 11: 1340. doi: 10.3389/fphar.2020.01340. PMC  7508056. PMID  33013372.
  6. ^ Cheung, LamLam (December 2013). The Emulsifying Properties of Cruciferin Rich and Napin Rich Protein Isolates From Brassica Napus L (Master of Science thesis). University of Saskatchewan. CiteSeerx10.1.1.848.5181.
  7. ^ Munir, A. (2000). "In silico studies and functional characterization of a napin protein from seeds of Brassica juncea" (PDF). International Journal of Agriculture and Biology. 19–1092. doi: 10.17957/IJAB/15.1247 (inactive 31 January 2024).{{ cite journal}}: CS1 maint: DOI inactive as of January 2024 ( link)
  8. ^ Mignone, G. (2022). "Isolation of the mustard Napin protein Allergen Sin a 1 and characterisation of its antifungal activity". Biochemistry and Biophysics Reports. 29 (101208): 101208. doi: 10.1016/j.bbrep.2022.101208. PMC  8777239. PMID  35079640.
  9. ^ Jyothi, T. C. (2007). "Napin from Brassica juncea: Thermodynamic and structural analysis of stability". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1774 (7): 907–919. doi: 10.1016/j.bbapap.2007.04.008. PMID  17544981.
  10. ^ a b Ericson, M. L.; Rödin, J.; Lenman, M.; Glimelius, K.; Josefsson, L. G.; Rask, L. (1986-11-05). "Structure of the rapeseed 1.7 S storage protein, napin, and its precursor". The Journal of Biological Chemistry. 261 (31): 14576–14581. doi: 10.1016/S0021-9258(18)66909-1. ISSN  0021-9258. PMID  3771543.
  11. ^ Perera, Suneru P.; McIntosh, Tara C.; Wanasundara, Janitha P. D. (2016-09-07). "Structural Properties of Cruciferin and Napin of Brassica napus (Canola) Show Distinct Responses to Changes in pH and Temperature". Plants. 5 (3): E36. doi: 10.3390/plants5030036. ISSN  2223-7747. PMC  5039744. PMID  27618118.



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