CP4 Plant Proteases from Biodiverse Sources
DOI:
https://doi.org/10.3407/rpn.v6i1cp4Keywords:
Proteases, Biodiversity, Ethnobotany, Proteolytic enzymes, PeptidasesAbstract
Proteolytic enzymes, also known as proteases or peptidases, are hydrolases that participate in all reactions that involve protein degradation, as they catalyze the hydrolysis of peptide bonds. Peptidases are found naturally in all living organisms and constitute between 1% and 5% of the genome. The catalytic type of peptidases is related to the chemical nature of the amino acids involved in the catalytic reaction. Consequently, the MEROPS [1] classification system groups them into cysteine, serine, threonine, aspartic, glutamic, and metalloproteases.
References
[1] RAWLINGS, N.D., et al. (2018). The MEROPS database of proteolytic enzymes, their substrates and inhibitors in 2017 and a comparison with peptidases in the PANTHER database. Nucleic Acids Res., 46, D624-D632.
[2] SINGH, G., et al. (2019). Biobleaching for Pulp and Paper Industry in India: Emerging Enzyme Technology. Biocatal. Agricul. Biotechnol., 17: 558–565.
[3] TORRES, M.J. et al. (2012). Characterization of the proteolytic system present in Vasconcellea quercifolia latex. Planta, 236:1471-84.
[4] ERRASTI, M.E. et al. (2018) Proteolytic extracts of three Bromeliaceae species as eco-compatible tools for leather industry. Environ. Sci. Pollut. Res. Int., 25:21459-21466.
[5] TREJO, S.A. et al., (2009). Sequencing and characterization of asclepain f: the first cysteine peptidase cDNA cloned and expressed from Asclepias fruticosa latex. Planta, 230: 319–328.
[6] RIOS SILVERA, R.I. et al., (2021) Standardized production of a homogeneous latex enzyme source overcoming seasonality and microenvironmental variables. Prep. Biochem. Biotech., 51(4): 375–385.
[7] SEQUEIROS, C. et al., (2005). Philibertain g I the most basic cysteine endopeptidase purified from the latex of Philibertia gilliesii Hook. et Arn. (Apocynaceae). The Protein J., 24: 445-53.
[8] CORRONS, M.A. et al., (2012) Milk clotting activity and production of bioactive peptides from whey using Maclura pomifera proteases”. LWT - Food Science and Technology, 47: 103-109.
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