Papain, a Plant Enzyme of Biological Importance: A Review

@article{Amri2012PapainAP,
  title={Papain, a Plant Enzyme of Biological Importance: A Review},
  author={Ez-Zoubir Amri and Florence A. Mamboya},
  journal={American Journal of Biochemistry and Biotechnology},
  year={2012},
  volume={8},
  pages={99-104}
}
  • E. Amri, F. Mamboya
  • Published 22 June 2012
  • Biology, Chemistry
  • American Journal of Biochemistry and Biotechnology
Papain is a plant proteolytic enzyme for the cysteine proteinase family cysteine protease enzyme in which enormous progress has been made to understand its functions. Papain is found naturally in papaya (Carica papaya L.) manufactured from the latex of raw papaya fruits. The enzyme is able to break down organic molecules made of amino acids, known as polypeptides and thus plays a crucial role in diverse biological processes in physiological and pathological states, drug designs, industrial uses… 

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References

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TLDR
This is the first comprehensive review on papaya that attempts to integrate so many aspects of this economically and culturally important fruit tree that should prove valuable for professionals involved in both research and commerce.
Antifungal effects of pawpaw seed extracts and papain on post harvest Carica papaya L. fruit rot
TLDR
Findings are hinged on non- chemical means of shelf life elongation of harvested pawpaw fruit in Africa and there seem to be no significant difference in activity between the extracts (aqueous seed extract and papain).
Peptidyl N-Nitrosoanilines: A Novel Class of Cysteine Protease Inactivators†,‡
TLDR
The covalent yet recoverable cysteine protease inactivation process offers mechanistic implications and endows this new family of inactivators with special properties that are suitable for the development of stable and stable protease inhibitors.
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TLDR
The complex structure of papain with CLIK148, which is a representative inhibitor from the CLIK series, is reported, which uses both prime and nonprime sites, which are important for the specific inhibitory effect on cathepsin L.
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TLDR
Analogs of the epoxysuccinyl peptide cysteine proteinase inhibitor, EP-475 (2a), in which the free carboxylate has been replaced by hydroxamic acid, amide, methyl ketone, hydroxyl, and ethyl ester functionalities, have been synthesized and show that a carbonyl-containing functionality is necessary for good activity.
Structure of papain refined at 1.65 A resolution.
Effect of Maturity Stage of Papaya Maradol on Physiological and Biochemical Parameters
Problem statement: Nowadays, the worldwide increase in diseases has motivated consumers to increase the intake of fruits and vegetables, in response to various research reports indicating that fruits
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TLDR
The specificity of the S(1)' subsite of the proteolytic enzyme papain has a predilection for hydrophobic residues, in particular l-leucine and l-tryptophan, which is manifest in both the binding and acylation steps.
Screening of Dioecious Papaya Hybrids for Papain Yield and Enzyme Activity
TLDR
An experiment was conducted to evaluate the performance of hybrids of dioecious papaya for papain yield and enzyme activity and revealed that the papain recove ry per f ruit was higher in P usa Dwarf X 9 -1(D) and 9-1 (D) X CO5 but the enzyme activity wasHigher in C O 5 X 9- 1(D).
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