3.4.22.2: papain
This is an abbreviated version!
For detailed information about papain, go to the full flat file.
Word Map on EC 3.4.22.2
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3.4.22.2
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cathepsins
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proteinases
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chymotrypsin
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pepsin
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cystatins
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bromelain
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igg
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hydrolysates
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cartilage
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immunoglobulin
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ficin
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pronase
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proteoglycans
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erythrocyte
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glycosaminoglycans
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alpha-chymotrypsin
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elastase
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neuraminidase
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chondroitin
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alcalase
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subtilisin
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latex
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thermolysin
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carica
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allergen
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articular
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agglutination
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collagenase
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emphysema
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plasmin
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kininogens
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fab\'2
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anti-d
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intra-articular
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bacteriocins
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pineapple
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legumains
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l-like
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pancreatin
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meromyosin
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dermatan
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emphysematous
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chondroitinase
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antiglobulin
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nutrition
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actin-activated
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medicine
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food industry
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enzyme-treated
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industry
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alloantibody
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subfragment-1
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analysis
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synthesis
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carlsberg
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biotechnology
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procathepsins
- 3.4.22.2
- cathepsins
- proteinases
- chymotrypsin
- pepsin
- cystatins
- bromelain
- igg
- hydrolysates
- cartilage
- immunoglobulin
- ficin
- pronase
- proteoglycans
- erythrocyte
- glycosaminoglycans
- alpha-chymotrypsin
- elastase
- neuraminidase
- chondroitin
- alcalase
- subtilisin
- latex
- thermolysin
- carica
- allergen
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articular
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agglutination
- collagenase
- emphysema
- plasmin
- kininogens
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fab\'2
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anti-d
-
intra-articular
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bacteriocins
- pineapple
- legumains
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l-like
- pancreatin
- meromyosin
- dermatan
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emphysematous
- chondroitinase
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antiglobulin
- nutrition
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actin-activated
- medicine
- food industry
-
enzyme-treated
- industry
-
alloantibody
-
subfragment-1
- analysis
- synthesis
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carlsberg
- biotechnology
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procathepsins
Reaction
Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1' =
Synonyms
Adolph's Meat Tenderizer, arbuz, CpXCP5, EC 3.4.4.10, enzeco papain, papain, papain-like cysteine protease, papain-like protease, papaine, papaya peptidase I, papaya proteinase 1, Papaya proteinase I, papayotin, PLCP, PLpro, PPI, summetrin, velardon
ECTree
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Application
Application on EC 3.4.22.2 - papain
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analysis
biotechnology
food industry
combination of ultrasound and papain is more beneficial for improving functional properties of meat compared with the individual treatment
industry
medicine
nutrition
synthesis
analysis
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study on the cross-sectional distribution of methylene blue and papain in porous silicon layers by TOF-SIMS. The larger Papain molecule distributes itself in a similar manner to methylene blue demonstrating larger molecules can be effectively incorporated into such pore structures
analysis
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study on the mixed micellar behavior of anionic surfactant, sodium dodecylsulfate, and cationic surfactant, dodecylethyldimethylammonium bromide, in aqueous solution of papain. The effect of concentration of papain on mixed micellar behavior indicates that with increase in the concentration of protein, the critical aggregation concentration and critical micellizationconcentration values increase. The unfolding of the polypeptide chain in the presence of mixed surfactant has been observed
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immobilization of papain and dehydration by n-propanol in low-water media at pH 6.4 and 25°C in 150 mM sodium phosphate buffer, stability is increased by solid state cysteine, overview
biotechnology
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papain immobilization on magnetic composite microspheres at pH 8.0 and 30°C, quantification and kinetics, overview, the immobilized enzyme exhibits better environmentally adaptability and reusability than the soluble enzyme
biotechnology
the enzyme plays a key role in biotechnology and has a range of important applications in cell isolation, leather, cosmetic, textiles, detergents, food, and pharmaceutical industries
biotechnology
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evaluation of toxic and mutagenic potential of papain and its potential antioxidant activity against induced-H2O2 oxidative stress in Escherichia coli strains by cytotoxicity assay, growth inhibition test, WP2-mutoxitest and plasmid-DNA treatment, and agarose gel electrophoresis. Papain exhibits negative results for all tests
biotechnology
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immobilisation of papain on gold nanorods enhances enzyme stability and efficiency, opening new opportunities for biotechnological applications
papain has many uses and functions in a variety of industries: clarifying beer, meat tenderization, preservation of spices, contact lens cleaners, detergents, pet food palatability, digestive aids, blood stain remover, blood coagulant and cosmetics
industry
the cotton fabric immobilized modified papain has potential applicationsin the functional textiles field
industry
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the enzyme with high biological activity and the decomposing ability is widely used in the lines of medical application, cell isolation, food, detergents, leather, textile, cosmetic and pharmaceutical industry
industry
catalytic properties of papain immobilized on hybrid nanoflowers are enhanced compared with that of free papain. The hybrid nanoflowers exhibit excellent reusability, high thermostability, long storage life and great potential in industrial applications
industry
immobilization on multi-walled carbon nanotubes is beneficial to the industrial applications because of its potential to be easily separated from the end product at the end of the reaction, reuse for multiple times and allow the development of multiple enzyme reaction system
industry
papain combined with chitosan-sodium alginate pretreated with the appropriate ultrasound can be effective technique for improving the activity of immobilized enzymes as a result of changes in its structure and intermolecular interactions. It is important to extend the application of chitosan-sodium alginate gel in the immobilized enzyme industry
medicine
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used in external treatment of hard tissue, wart and scar tissue removal, acne treatment, depilation, skin cleansing treatment, inclusing in toothpaste. Papain is used in preparation of Tyr derivatives which are used for treatment of Parkinsonism and for the preparation of tetanus vaccines and immunoglobulin samples for intravenous injection
medicine
papain is widely used for many medical and para-medical purposes such as to assist protein digestion in chronic dyspepsia, gastric fermentation, gastritis, removal of necrotic tissue, preparation of tyrosine derivatives for the treatment of Parkinsonism, preparation of tetanus vaccines, skin cleansing agents and acne treatment
medicine
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effects of papain and neuraminidase enzyme treatment on electrohydrodynamics and IgG-mediated agglutination of type A red blood cells. Papain treatment results in a significant reduction of the hydrodynamic permeability of the external soft glycoprotein layer of the cells, reflecting a significant decrease in soft surface layer thickness and a loss in cell surface integrity/rigidity
medicine
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entrapment of papain into a polymeric matrix in order to obtain a drug delivery system that can be used as medical device after sterilization by gamma radiation. Papain release and its activity in membranes containing 2% w/w papain in a silicone dispersion is not significantly affected by gamma irradiation
medicine
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method for internalization of monoclonal antibodies based on papain digestion followed by flow cytometry. This method can identify whether the binding monoclonal antibody has internalized into the cell, with an additional advantage of accurately quantifying the internalized monoclonal antibody without altering cell morphology after papain digestion. The methodology can facilitate understanding of the efficiency of monoclonal antibody internalization and evaluation of the targeted killing capacity of the monoclonal antibody
medicine
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study wether glucosamine modulates the immune and inflammatory responses to joint injury in organs proximal to glucosamine absorption using a papin-injected knee mouse model. Papain significantly degrades the proteoglycans in the injected knees by 2 days. Cartilage proteoglycan content is significantly higher in glucosamine-treated, papain-injected knees at Day 14. The peak concentration of serum pro-inflammatory cytokines occurrs earlier and decreases sooner in the injected, glucosamine-supplemented mice
medicine
a potential new self-emulsifying drug delivery system with mucolytic features for oral administration is developed. Using hydrophobic ion pairing, papain can be successfully included in the system. Within all formulations papain exhibits a mucolytic effect and accelerates a higher permeation in porcine intestinal mucus. Additionally a prolonged mucosal residence confirms that upon incorporation of enzyme, self-emulsifying drug delivery systems are awarded with the ability to overcome the intestinal barrier more easily. This system can be presented as a promising carrier capable to transport a therapeutic ingredient across the mucus barrier and finally improve its bioavailability
medicine
dental plaque is a causative factor for oral disease and a potential reservoir for respiratory infection in the elderly. Therefore, there is a critical need for the development of effective methods to remove oral biofilm. Proteases reduce oral biofilm in vivo in elderly subjects. Tablets containing actinidin remove tongue coating in elderly subjects. Oral Actinomyces biofilm is significantly reduced by the proteases papain, actinidin and trypsin. Papain and trypsin effectively digest the major fimbrial proteins, FimP and FimA, from Actinomyces. Actinidin, papain and trypsin reduce multispecies biofilm that is reconstructed in vitro. Papain and trypsin inhibit formation of multispecies biofilm in vitro
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papain is used in the preparation of fish protein concentrates from fish waste
nutrition
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used in the tenderisation of meat by its action on connective tissue and muscle protein. Beef is the only meat that is routinely subjected to papain tenderisation and the application of this technology is almost exclusively restricted to the USA
nutrition
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the enzyme is used for the development of roast beef-like flavours by partial hydrolysis of proteins
nutrition
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papain is used in the brewing process for two main purposes: use in chillproofing and use in the mash tun to uncrease the yield of extract and therefore decrease malt consumption. The enzyme can be used in the production of specialized fish protein concentrate for use as a milk replacer when feeding calves and piglets. The enzyme is used to improve the protein dispersibility index of soya flour. Treatment of oil seed cake to incrase the nitrogen solubility index and/or the protein dispersibility index
nutrition
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used extensively in food processing especially in tenderization of meat
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use as catalyst in asymetric synthesis of acyl derivatives and in peptide synthesis
synthesis
chemical modification of papain using different anhydrides of 1,2,4-benzenetricarboxylic and pyromellitic acids and immobilization on cotton fabric results in immobilized papain with optimum pH shifted from 6.0 to 9.0. Compared with immobilized native papain, the thermal stability and the resistance to alkali and washing detergent of immobilized modified enzyme are improved considerably. When the concentration of detergent is 20 mg/ml, the activity of the immobilized pyromellitic papain retains about 40% of its original activity, whereas the native papain is almost inhibited
synthesis
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enzymatic hydrolysis of casein to produce free amino acids by papain in a two-phase system, which is composed of n-propanol, NaCl and water. In this system, the top phase contains more n-propanol and the bottom phase contains more NaCl and water. Papain and casein are mainly distributed in bottom phase, and free aromatic amino acids tyrosine, tryptophan and phenylalanine produced by enzymatic hydrolysis aere mainly in top phase. When the two-phase system consists of 44% n-propanol, 60 g/l NaCl, 0.15 g/l papain and 13 g/l casein at 55°C and pH 5.6, the transformation yield is 99.5%
synthesis
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Fab antibody fragment production and purification by papain digestion of an intact monoclonal antibody. After digestion, separation of the Fab fragment from the Fc fragment and residual intact antibody is achieved using protein A affinity chromatography. The Fab fragments are of high quality suitable to produce diffraction quality crystals suitable for X-ray crystallographic analysis
synthesis
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immobilization of papain on Sepharose 6B in the presence of different concentrations of cysteine affect the enzyme activity depending on cysteine concentration. The maximum specific activity is observed when papain was immobilized with 200 mM cysteine. The immobilization process results in significant enhancement of stability to temperature and extreme pH. After immobilization, the optimum temperature of papain activity increases by 20 degrees from 60 to 80°C and its optimum pH activity shifts from 6.5 to 8.0. Catalytic efficiency and specific activity of the immobilized enzyme do not significantly change after immobilization