Comparative study of the stability of free and modified papain incorporated in topical formulations

Pinto, Claudinéia Aparecida Sales de Oliveira; Lopes, Patrícia Santos; Sarruf, Fernanda Daud; Polakiewicz, Bronislaw; Kaneko, Telma Mary; Baby, André Rolim; Velasco, Maria Valéria Robles

doi:10.1590/s1984-82502011000400012

Cited by 10 publications

(11 citation statements)

References 17 publications

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“…Multiple attempts have been made to stabilize the papain, including covalent immobilization, interaction with metal ions, copolymerization with glutaraldehyde, immobilization in agarose, covalent binding with polyethersulfone, modification with succinic anhydride, simple adsorption in Celite ® , ion absorption, adsorption on nylon-based immobilized copper ion affinity membrane [ 21 ], adsorption on electrospun nylon nanofiber as affinity membrane [ 22 ], inclusion in starch-based gel, and incorporation in nitrile fiber enriched with amino groups, as well as immobilization on the surface of cotton fabric [ 23 ], sepharose, nanoparticles, incorporation in niosomes, nanospheres, liposomes, and many others [ 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 ]. In some of the latest assays, both antibacterial and anti-biofilm activities of immobilized papain have been reported [ 6 , 34 ].…”

Section: Introductionmentioning

confidence: 99%

Biochemical Properties and Anti-Biofilm Activity of Chitosan-Immobilized Papain

et al. 2021

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Chitosan, the product of chitin deacetylation, is an excellent candidate for enzyme immobilization purposes. Here we demonstrate that papain, an endolytic cysteine protease (EC: 3.4.22.2) from Carica papaya latex immobilized on the matrixes of medium molecular (200 kDa) and high molecular (350 kDa) weight chitosans exhibits anti-biofilm activity and increases the antimicrobials efficiency against biofilm-embedded bacteria. Immobilization in glycine buffer (pH 9.0) allowed adsorption up to 30% of the total protein (mg g chitosan−1) and specific activity (U mg protein−1), leading to the preservation of more than 90% of the initial total activity (U mL−1). While optimal pH and temperature of the immobilized papain did not change, the immobilized enzyme exhibited elevated thermal stability and 6–7-fold longer half-life time in comparison with the soluble papain. While one-half of the total enzyme dissociates from both carriers in 24 h, this property could be used for wound-dressing materials design with dosed release of the enzyme to overcome the relatively high cytotoxicity of soluble papain. Our results indicate that both soluble and immobilized papain efficiently destroy biofilms formed by Staphylococcus aureus and Staphylococcus epidermidis. As a consequence, papain, both soluble and immobilized on medium molecular weight chitosan, is capable of potentiating the efficacy of antimicrobials against biofilm-embedded Staphylococci. Thus, papain immobilized on medium molecular weight chitosan appears a presumably beneficial agent for outer wound treatment for biofilms destruction, increasing antimicrobial treatment effectiveness.

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Section: Introductionmentioning

confidence: 99%

Biochemical Properties and Anti-Biofilm Activity of Chitosan-Immobilized Papain

et al. 2021

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“…Papain (EC 3.4.22.2) is a proteolytic enzyme extracted from the latex of papaya ( Carica papaya ) [1]. This enzyme has a wide range of substrate specificity, preferably acting on peptide bonds involving arginine and lysine or phenylalanine, leucine and glycine residues [1, 2]. Papain is the most commercialized enzyme in the protease market, outselling other plant‐based and microbial proteases [3].…”

Section: Introductionmentioning

confidence: 99%

In vitro effect on the proteolytic activity of papain with proteins of the skin as substrate

Trevisol

Henriques

Cesca

et al. 2022

Intern J of Cosmetic Sci

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Objective This work aims to evaluate the effects of enzyme concentration, pH, temperature and time course degree of hydrolysis (DH) of papain regarding further development of pharmaceutical and cosmetic formulations. Methods The hydrolysis of casein, collagen, keratin and porcine skin at pH and temperature ranges of the human skin was evaluated. Also, low contact times of enzyme–substrate were studied. The incorporation of 3mM of cysteine improved the caseinolytic (PU), collagenolytic (CU) and keratinolytic (KU) activities of papain. Results: In general, the increase from 0.1 to 1.0 or 2.0 mgmL−1 of papain improved PU, CU and KU. When 2.0 mgmL−1 of papain was used, the highest DH of casein, collagen and keratin was obtained at 240min (14%, 35% and 6% respectively). The decrease in pH and temperature reduced all proteolytic activities, but papain maintained at least 50% and 40% of its activity at 26°C and pH 4.5 respectively. Scanning electron micrographs of the surface of the skin showed that papain application had exfoliating activity. Conclusion This preformulation study demonstrated that papain concentration, time of application and pH of the product should be evaluated when developing a product to promote the hydrolysis of the proteins of the skin.

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“…This study was aimed at comparing the moisturizing, tensor and transepidermal water loss effects of the peel‐off facial mask, after its application and removal of the skin, with an oil‐in‐water (o/w) emulsion . Both formulations were made with and without soybean extract fermented by Bifidobacterium animale (5% w/w), obtaining four formulations.…”

Section: Introductionmentioning

confidence: 99%