microbial proteases for by-product valorization through hydrol- operating conditions (temperature, pH, salinity, and organic

Overview

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Key numbers

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proteases is in continuous growth because they represent 60 % peptidases, the nucleophile is activated by water
US$, showing a compound annual growth rate (CAGR) of 6.1 % that share sufficient sequence homology (amino acidic
catalytic dyad. Three clans, (SA, SB, and SC) share a catalytic ature up to 55 °C. APs show a molecular weight range of 35–
120 kDa (most of them lies within the 60–80 kDa range). The highlighting papain, bromelain, ficin, and actinidin (see Table 1).
exceptions are Ara12 from A. thaliana, RSIP from maize, and C1 Table 2 shows emerging serine and aspartic endopeptidases
Table 1. Traditional plant proteases with industrial applications.
Table 2. Emerging serine and aspartic plant endopeptidases with industrial applications reported in recent years.
main steps: 1. Nucleophilic attack by an activated water vegetable biomass (latex, flowers, fruits, roots) using traditional
consists of ANA (α-naphthaleneacetic acid) and 0.5 ppm of BA promotors systems (similar to those used in micropropagation
account for the techno-economic evaluation. stability higher than 75–80 % over a wide range of pH (4–10)
proteolytic activity (1 % casein substrate) was observed in that pathogens such as insects and fungi and most belong to the
The authors noted that there are promising plants with now). Table 4 shows the main structural facts of the most
nein), Apocynaceae (cryptolepain, ervatamins A, B, C, heynein, subtilis.(66) Macluralisin’s N-terminal sequence shares 30 % ho-
P, La1, La2, La3 Lc, T1, T2, T3, T4, milin) have been identified.(54) Tritirachium album whereas Taraxalisin’s has 40 % of its residues
proteases. However, APs have fewer inhibitors. Table 3 shows dase A, alcalase Novo), was discovered by Linderstrøm-Lang
Flowers are also a suitable source of PPs.(55–57) For example, plakalbumin. The similarity of catalytic and binding site geo-
considered valuable vegetable protease sources. Within this activity.(67)
phase polyethylene glycol/dextran system, reaching 97.3 % yield showed a high degree of identity with that of Subtilisin-like
(PEG) and 4.5 % of NaCl at pH 7.5).(58) The proteases showed to with any sequence of known plant serine proteases.
be active for azocasein hydrolysis, indicating that mango peel Latex cysteine proteases are in the range from 21 to 29 kDa
could be an effective source of natural enzymes considering the in molecular weight, are stable in the range 3–12 of pH and up
Table 3. Proteases isolated from plant latices.(54,59–61)
Table 4. Some serine proteases in plant latices.
complete description of properties of several latex proteases.(54) substrate solution (2 % casein in 10 mm. Tris-Cl buffer pH 8.0)
Ervatamin C has a similarity of 66 % to Ervatamin B and 50 % addition of an equal volume of 10 % chilled trichloroacetic acid
crussasiva L. and shows a high identity with Funastrain CII to 10 mL solution containing 1 % (w/v) casein, 0.05 m acetate,
(87 %) and Asclepain F (86 %). Araujiain HI, HII, and HIII show 0.05 m phosphate, and 5.0 × 10 m EDTA 0,05 mL of enzyme
partial homology (36–48 %) with other plant cysteine protei- were added. Two-milliliter aliquots were removed at 0, 10, 20,
nases. and 30 minutes and added to 3.0 mL of 5 % trichloroacetic acid
no homology at all to up to 90 % homology. Within this context, Depending on the source of the protease and its degree of
Table 6 presents a comparison of the activity of different experimental conditions and the additives (cysteine, group 2
Table 5. Cysteine proteases from plant latices.
Table 6. Examples of degree of hydrolysis (%) or Units mg 1 protein for different proteases with casein, whey concentrate, or milk as substrates.
(72) Actinidin Whey concentrate – 15–70 5h 3.7–15 %
(73) Bromelain Casein 1 % 5.1 35 30 min 41.7 U mg 1
Euphorbia synudenium Casein 2 % 8 50 20 min 9.44 U mg 1
Carica papaya Casein 2 % 8 50 20 min 0.935 U mg 1
Calotropis gigantea Casein 2 % 8 50 20 min 0.618 U mg 1
Calotropis procera Casein 2 % 8 50 20 min 0.82 U mg 1
Plumberia Rubera Casein 2 % 8 50 20 min 1.03 U mg 1
Ficus religiosa Casein 2 % 8 50 20 min 2.17 U mg 1
(70) Araujia hortorum latex Casein 1 % 8 45 2 min 12.8 U mg 1

Methods (brief)

finally, gel filtration coupled to HPLC system. PPA (with a 4.1.2. Hydrolysis of Protein-Based Substrates
samples treated with crude enzyme was 65.7 %, using an work, Jayawardana et al. investigated the effect of actinidin on
enzymatic concentration of 0.03 % wt. at 37 °C after 5 h. Mean- the hydrolysis of gluten proteins and digestion-resistant gluten
digestion. Cucumis melo protease exhibited the highest activity * Collagen V: it is commonly found in hair, cell surfaces, and
Langmuir isotherm model. The immobilized papain sample methods.
enzyme concentration between 2 and 5 %. The optimal activity adsorbed on the hair and the samples becoming thinner. The
Actidin Kiwifruit Healing of neuropathic diabetic foot ulcer, increase protein digestion and ameliorate of (264)
Synthetic * The chemical structure of the matrix could be designed (e. g., nylon grafted with * Papain (p(HEMA-EGDMA))
Berenguer-Murcia, M. R. Kamli, O. Tavano, R. Fernandez-Lafuente, Int. J. (309) D. Hyndman, R. Burrell, G. Lever, T. G. Flynn, Biotechnol. Bioeng. 1992,

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Commit	Date	Change	Description
b01ec52c	2026-08-04	major	2 sections added
d49e450f	2026-08-03	major	5 sections added; narrative text revised