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Information on EC 3.4.22.33 - Fruit bromelain and Organism(s) Ananas comosus and UniProt Accession O23791
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3.4.22.33 Fruit bromelainSpecify your search results
The taxonomic range for the selected organisms is: Ananas comosus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins with broad specificity for peptide bonds. Bz-Phe-Val-Arg-/-NHMec is a good synthetic substrate, but there is no action on Z-Arg-Arg-NHMec (c.f. stem bromelain)
Synonyms
bromelin, bromelain a, fruit bromelain, fastuosain, pinase, bromelase, bromelain b, fruit bromelain fa2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ananase
-
-
-
-
Bromelain, juice
-
-
-
-
Bromelase
-
-
-
-
Bromelin
Extranase
-
-
-
-
Fruit bromelain
Fruit bromelain FA2
-
-
-
-
Juice bromelain
-
-
-
-
Pinase
-
-
-
-
Traumanase
-
-
-
-
additional information
-
c.f. stem bromelain, enzyme belongs to the papain superfamily
Bromelin
-
-
-
-
Fruit bromelain
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-00-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzyl-Phe-Val-Arg-4-nitroanilide + H2O
benzyl-Phe-Val-Arg + 4-nitroaniline
preferred substrate of fruit bromelain
-
-
?
benzyloxycarbonyl-Arg-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + 4-nitroaniline
-
-
-
?
Benzoyl-Gly-Gly-Lys + H2O
?
-
enzyme form FBA is much more active than FBB
-
-
?
benzoyl-Phe-Val-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
convenient substrate for fruit bromelain, scarcely affected by stem bromelain
-
-
?
benzoyl-Phe-Val-Arg-p-nitroanilide + H2O
benzoyl-Phe-Val-Arg + p-nitroaniline
-
-
-
-
?
Benzyloxycarbonyl-Ala-Leu + H2O
Benzyloxycarbonyl-Ala + Leu
-
enzyme form FBA is much more active than FBB
-
-
?
benzyloxycarbonyl-Arg-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + p-nitroaniline
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
-
enzyme form FBA is much more active than FBB
-
-
?
Benzyloxycarbonyl-Gly-Val + H2O
Benzyloxycarbonyl-Gly + Val
-
enzyme form FBA is much more active than FBB
-
-
?
bromelain + H2O
?
-
rapid self-digestion in aqueous solution, can be prevented by addition of alpha2-macroglobulin
-
?
Carbobenzoxy-Gly-Ala + H2O
Carbobenzoxy-Gly + Ala
-
enzyme form FBA is much more active than FBB
-
-
?
Nalpha-Benzoyl-Arg amide + H2O
Nalpha-Benzoyl-Arg + NH3
-
-
-
-
?
Nalpha-Benzoyl-DL-Arg 4-nitroanilide + H2O
Nalpha-Benzoyl-DL-Arg + 4-nitroaniline
-
-
-
-
?
angiotensin II + H2O
hydrolyzed angiotensin II
-
cleavage between Tyr4-Ile5
cleavage between Tyr4-Ile5
?
angiotensin II + H2O
hydrolyzed angiotensin II
-
cleavage between Tyr4-Ile5
cleavage between Tyr4-Ile5
?
bradykinin + H2O
fragments of bradykinin
-
cleavage between Gly4-Phe5 and Phe5-Ser6
cleavage between Gly4-Phe5 and Phe5-Ser6
?
bradykinin + H2O
fragments of bradykinin
-
cleavage between Gly4-Phe5 and Phe5-Ser6
cleavage between Gly4-Phe5 and Phe5-Ser6
?
casein + H2O
?
-
enzyme is assayed using casein as a substrate with Coomassie dye to track completion of hydrolysis of casein, casein is hydrolysed to completion leading to a brown coloured solution, assay method development as a Bradford dye-binding-bromelain-casein system as an assay for heavy metals, based on colour development and its inhibition by Hg2+ and Cu2+
-
-
?
additional information
?
-
-
enzyme catalyzes synthesis of acylamino acid anilides
-
-
?
additional information
?
-
-
bromelain has a profound immunmodulatory effect, overview, bromelain affects blood coagulation, fibrinolysis, and platelet functions, mechanism, overview
-
?
additional information
?
-
-
enzyme is scarcely able to hydrolyze benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide
-
-
?
additional information
?
-
-
bromelain is a cysteine protease containing a single thiol group in the active sites
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
bromelain has a profound immunmodulatory effect, overview, bromelain affects blood coagulation, fibrinolysis, and platelet functions, mechanism, overview
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
noncompetitive inhibition at pH 3.5, while both K-and V-type activations of bromelain are observed in the presence of 0.5 mM Ca2+ at pH 4.5 and pH 7.5
additional information
additional information
modulation of fruit bromelain by divalent ions is pH dependent
additional information
-
poor or no inhibition by ions K+, Ca2+, Mg2+, Mn2+, Co2+, Bo3+, Al3+, Cr2+, Ni2+, Sn2+, Ag+, Fe2+, Cd2+, Zn2+, W3+, Se2+, As3+, and Pb2+, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
noncompetitive inhibition at pH 3.5, while both K-and V-type activations of bromelain are observed in the presence of 0.5 mM Ca2+ at pH 4.5 and pH 7.5
Cu2+
competitive inhibition at pH 3.5 with 0.6 mM Cu2+, which changes to an uncompetitive inhibition at pH 4.5 and pH 7.5
cystatin
an extended AE-rich N-terminal trunk in secreted pineapple cystatin enhances inhibition of fruit bromelain and is posttranslationally removed during ripening, The AE-rich N-terminal trunk is required to inhibit fruit bromelain (above 95%), whereas its removal decreases inhibition to 20%. Recombinant cystatin containing the complete AE-rich N-terminal trunk and recombinant medium pineapple cystatin effectively inhibit bromelain compared to recombinant core pineapple cystatin
-
additional information
stability of bromelain in the presence of EDTA and sodium benzoate
-
additional information
stability of bromelain in the presence of EDTA and sodium benzoate
-
additional information
stability of bromelain in the presence of EDTA and sodium benzoate
-
additional information
stability of bromelain in the presence of EDTA and sodium benzoate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
high-pressure treatment of fruit bromelain with 300 MPa, at 20°C for 20 min: high pressure processing (HPP) affects the fibrinolytic activity of fruit bromelain in vivo, overview. Compared with untreated fruit bromelain, the fibrinolytic activity of high-pressure processing-treated fruit bromelain is obviously increased which might be attributed to the increase of alpha-helix and the exposure of tryptophan residues and tyrosine residues, overview. High-pressure processing-treated fruit bromelain shows an increase (7.67%) in alpha-helix and its fluorescence intensities are increased by 42.5% and 78.7% at the excitation wavelength of 295 nm and 280 nm, respectively
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics, kinetic modeling, detailed overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
inhibition kinetics, detailed overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1050.57
extracted crown bromelain, pH 6.0, 37°C, with substrate casein
1519.85
extracted pulp bromelain, pH 6.0, 37°C, with substrate casein
2512.44
purified native enzyme, pH and temperature not specified in the publication
1365.77
extracted peel bromelain, pH 6.0, 37°C, with substrate casein
additional information
4429.0 U/ml at pH 4.5, crude bromelain extract from fruit pulp
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.9
6.5
7.5
7.7
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
55
59
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 60
-
most suitable hydrolysate temperature of casein acids for bromelain is 50-60°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
pulp enzyme; an unexplored French Guiana variety, collected in 1993
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
bromelain is a mixture of bromelain A and B, the proteolytic enzymes of pineapple fruit
-
stem bromelain possess better gelatin digestion units (GDU) activity over fruit bromelain
additional information
analysis of bromelain activity in different Ananas comosus parts and tissues, overview
additional information
analysis of bromelain activity in different Ananas comosus parts and tissues, overview
additional information
-
bromelain is a crude extract containing a complex mixture of several components, such as different thiol-endopeptidases, phosphatases, glucosidases, peroxidases, cellulases, glycoproteins and carbohydrates, as well as several proteinase inhibitors
additional information
analysis of bromelain activity in different Ananas comosus parts and tissues, overview
additional information
analysis of bromelain activity in different Ananas comosus parts and tissues, overview
additional information
-
determination of bromelain protease activity in different tissues of pineapple of the Morris variety, overview. The flesh of the pineapple is the largest portion (w/w) for both Morris with crown and no crown followed by peel, core, stem and crown. The bromelain extracted from the peel exhibits high bromelain activity , only slightly lower than the flesh. Pineapple waste such as peels, which contribute to almost 30% of pineapple waste, can be a good source of bromelain
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
antiproliferative effect of bromelain from different tissues against B16F10 murine melanoma cells, overview
additional information
physiological function
antiproliferative effect of bromelain from different tissues against B16F10 murine melanoma cells, overview
physiological function
bromelain enzyme from pineapple fruit acts as an antiviral agent against HIV, hepatitis C and human papiloma virus. Patients are given two glasses of fresh juice from pineapple fruits per day resulting in reduced human immunodeficiency virus (HIV) load. Bromelain might cause some damage on the virus envelope protein structural components. Direct contact of bromelain enzymes from fruit powder with HI viruses causes morphological changes on the viruses
physiological function
bromelain is capable of unhairing of cow skin in solid state fermentation
physiological function
small peptides are separated from larger peptides and proteins by fruit bromelain in the human digestive tract, the peptides are capable of destabilizing and desaggregating insulin aggregates (e.g. B23-B30 des-octapeptide) to oligomers. The peptides GG and AAA serving as negative controls show no potency in destabilization of aggregates. Disaggregation potency of the peptides wis also observed when insulin is deposited on Hep-G2 liver cells where no formation of toxic oligomers occurs. Deposition of insulin aggregates in human body leads to dysfunctioning of several organs. Amyloidogenic des-octapeptide (B23-B30 of insulin) incapable of cell signaling also show cytotoxicity similar to insulin. This toxicity can also be neutralized by bromelain derived peptides. Disaggregated insulin has a structure distinctly different from that of its hexameric (native) or monomeric states, FT-IR and far-UV circular dichroism analysis. Ability of auto digested peptides from bromelain to act as an inhibitor of amyloid formation
additional information
comparative structural analysis of fruit and stem bromelain from Ananas comosus, structure homology modelling, model domain organisation, overview. The proteolytic fraction of pineapple stem is termed stem bromelain, while the one presents in the fruit is known as fruit bromelain (EC 3.4.22.33). NCBI conserved domain analysis reveals two domains of fruit and stem bromelain: cathepsin propeptide inhibitor (I29) and peptidase C1
additional information
-
comparative structural analysis of fruit and stem bromelain from Ananas comosus, structure homology modelling, model domain organisation, overview. The proteolytic fraction of pineapple stem is termed stem bromelain, while the one presents in the fruit is known as fruit bromelain (EC 3.4.22.33). NCBI conserved domain analysis reveals two domains of fruit and stem bromelain: cathepsin propeptide inhibitor (I29) and peptidase C1
additional information
effects of bromelain on the pro-wound healing activities and the regenerative properties of mesenchymal stem cells, overview. The combination of bromelain and dexamethasone sodium phosphate induces a great activation of mesenchymal stem cells with an increase in hyaluronan and collagen production and antiinflammatory cytokines release, real-time polymerase chain reaction analysis of extracellular matrix proteins and remodeling enzymes in human mesenchymal stem cells, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BROM1_ANACO
351
1
39055
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
27000
-
x * 23000, Ananas comosus, enzyme form FBA, SDS-PAGE, x * 27000, Ananas comosus, enzyme form FBB, SDS-PAGE
31000
23000
-
x * 23000, Ananas comosus, enzyme form FBA, SDS-PAGE, x * 27000, Ananas comosus, enzyme form FBB, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 23000, Ananas comosus, enzyme form FBA, SDS-PAGE, x * 27000, Ananas comosus, enzyme form FBB, SDS-PAGE
additional information
comparative structural analysis of fruit and stem bromelain from Ananas comosus
additional information
-
comparative structural analysis of fruit and stem bromelain from Ananas comosus
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-4
bromelain retains 75% of its activity when stored without preservative at -4°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
analysis of the stability of fruit bromelain in fruit pulp within a high-pressure domain of 0.1-600 MPa/30-70°C/1 s-30 min. The pulse effect is quantified as a function of pressure, temperature, pressure build-up and decompression times. A maximum of 60% reduction in FBM activity is obtained after a single pulse of 600 MPa/70°C. Upon applying nth order model, the obtained reaction order (n) for thermal (0.1 MPa/30-70°C) and high-pressure (100-600 MPa/30-70°C) inactivation is 1.1 and 1.2, respectively, inactivation rate constant, isothermal inactivation at atmospheric pressure, detailed overview. The activation energy is nonlinearly dependent on pressure, whereas the activation volume is linearly related to temperature. The empirical model appears to be more realistic than those from the log-linear kinetics. At 600 MPa/70°C, the first-order kinetics predict that 90% of initial FBM activity will be reduced after 46 min of pressure hold period, whereas, the empirical model predicts a dwell time of only 26 min for the same. Modelling
incubation with trypsin (1 mg/ml, 1 h, 37°C) results in 12% loss of activity (with benzyloxycarbonyl-Arg-Arg-p-nitroanilide as substrate) at bromelain concentration of 10 mg/ml , but has no effect on activity at bromelain concentrations of 100 mg/ml
-
proteolytic activity of solutions containing either 10 mg/ml or 100 mg/ml bromelain in water or 100 mg/ml NaHCO3 is not changed against benzyloxycarbonyl-Arg-Arg-p-nitroanilide and benzoyl-Phe-Val-Arg-p-nitroanilide substrate by four freeze/thaw cycles
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 7.23fold from fruits by ammonium sulfate fractionation, dialysis, and anion exchange chromatography
native enzyme from fruits by ion exchange chromatography and ultrafiltration
native enzyme partially from ripe fruits by lyophilization and gel filtration
bromelain from pineapple stem and skin are recovered by a PEG 4000/phosphate aqueous two-phase systems (ATPs) liquid-liquid extraction
-
high-speed counter-current chromatography coupled with the reverse micelle solvent system consisting of 0.10 g/ml cetyltrimethylammonium bromide (CTAB)/isooctane-hexylalcohol and 0.05 M sodium phosphate buffer is successfully applied to separate bromelain from pineapple fruit
-
using centrifugation, salt precipitation technique, dialysis, ion-exchange chromatography. Ion exchange chromatography using diethylaminoethyl cellulose (DEAE) anion exchangers maintain the structural integrity of purified bromelain and thereby the product exhibits better proteolytic activity than crude extract
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
bromelain has gained wide acceptance and compliance as a phytotherapeutical drug. Cysteine proteases in pineapple (Ananas comosus) plants are phytotherapeutical agents that demonstrate antiedematous, anti-inflammatory, anti-thrombotic and fibrinolytic activities
pharmacology
bromelain is pharmacologically active against B16F10 melanoma cells with complete inhibition of tumor cell proliferation in vitro
medicine
pharmacology
additional information
medicine
-
bromelain can be used as a phytotherapy agent in several aspects, overview
medicine
bromelain exhibits various fibrinolytic, anti-edematous, antithrombotic, and anti-inflammatory activities supporting its application for many therapeutic benefits. Effects of bromelain on the pro-wound healing activities and the regenerative properties of mesenchymal stem cells. The combined use of bromelain and dexamethasone sodium phosphate stimulated the pro-wound healing activities and the regenerative properties of mesenchymal stem cells better than bromelain and dexamethasone alone
pharmacology
-
use as additive to prevent lymphedema by reducing lymphocongestion, detritus, viscosity of the exsudate and stimulation of phagocytosis of associated leukocytes, use as additive for radiotherapy and surgery due to wound healing effect and reductive effect on inflammation and edema, use as additives for chemotherapy due to inhibitory effects on malignant growth of tumor cells
pharmacology
bromelain is pharmacologically active against B16F10 melanoma cells with complete inhibition of tumor cell proliferation in vitro
additional information
bromelain can be useful in leather production industry for unhairing of skin
additional information
high pressure processing treatment can effectively enhance the fibrinolytic activity of fruit bromelain in vivo and increase the added-value as well as market competitiveness of pineapple-derived products. High-pressure processing-treated fruit bromelain can potentially be used in the development of a functional food that can prevent thrombosis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ota, S.; Horie, K.; Hagino, F.; Hashimoto, C.; Date, H.
Fractionation and some properties of the proteolytically active components of bromelains in the stem and the fruit of the pineapple plant
J. Biochem.
71
817-830
1972
Ananas comosus
Ota, S.; Muta, E.; Katahira, Y.; Okamoto, Y.
Reinvestigation of fractionation and some properties of the proteolytically active components of stem and fruit bromelains
J. Biochem.
98
219-228
1985
Ananas comosus
Rowan, A.D.; Brzin, J.; Buttle, D.J.; Barrett, A.J.
Inhibition of cysteine proteinases by a protein inhibitor from potato
FEBS Lett.
269
328-330
1990
Ananas comosus
Suh, H.J.; Lee, H.; Cho, H.Y.; Yang, H.C.
Purification and characterization of bromelain isolated from pineapple
Han'guk Nonghwa Hakhoechi
35
300-307
1992
Ananas comosus
-
Yamada, F.; Takahashi, N.; Murachi, T.
Purification and characterization of a proteinase from pineapple fruit, fruit bromelain FA2
J. Biochem.
79
1223-1234
1976
Ananas comosus
Sasaki, M.; Kato, T.; Iida, S.
Antigenic determinant common to four kinds of thiol proteases of plant origin
J. Biochem.
74
635-637
1973
Ananas comosus
Toro-Goyco, E.; Rodriguez-Costas, I.
Immunochemical studies on pinguinain. A sulfhydryl plant protease
Arch. Biochem. Biophys.
175
359-366
1976
Ananas comosus, Bromelia pinguin
Maurer, H.R.
Bromelain: biochemistry, pharmacology and medical use
Cell. Mol. Life Sci.
58
1234-1245
2001
Ananas comosus
Rowan, A.D.
Fruit bromelain
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
2
1137-1138
2004
Ananas comosus
-
Hale, L.P.; Greer, P.K.; Trinh, C.T.; James, C.L.
Proteinase activity and stability of natural bromelain preparations
Int. Immunopharmacol.
5
783-793
2005
Ananas comosus
Hemavathi, A.B.; Hebbar, H.U.; Raghavarao, K.S.
Reverse micellar extraction of bromelain from Ananas comosus L. Merryl
J. Chem. Technol. Biotechnol.
82
985-992
2007
Ananas comosus (O23791)
-
Shukor, M.Y.; Masdor, N.; Baharom, N.A.; Jamal, J.A.; Abdullah, M.P.; Shamaan, N.A.; Syed, M.A.
An inhibitive determination method for heavy metals using bromelain, a cysteine protease
Appl. Biochem. Biotechnol.
144
283-291
2008
Ananas comosus
Neuteboom, L.W.; Matsumoto, K.O.; Christopher, D.A.
An extended AE-rich N-terminal trunk in secreted pineapple cystatin enhances inhibition of fruit bromelain and is posttranslationally removed during ripening
Plant Physiol.
151
515-527
2009
Ananas comosus (O23791), Ananas comosus
Liang, H.; Li, M.; Shi, M.; Liao, A.; Wu, R.
Study on the stability of fruit bromelain
Adv. Mater. Res.
421
19-22
2012
Ananas comosus
-
Ferreira, J.; Bresolin, L.; Silveira, E.; Tambourgi, E.
Purification of bromelain from ananas comosus by PEG/phosphate ATPS
Chem. Eng. Transact.
24
931-936
2011
Ananas comosus
-
Yin, L.; Sun, C.; Han, X.; Xu, L.; Xu, Y.; Qi, Y.; Peng, J.
Preparative purification of bromelain (EC 3.4.22.33) from pineapple fruit by high-speed counter-current chromatography using a reverse-micelle solvent system
Food Chem.
129
925-932
2011
Ananas comosus
Gautam, S.; Mishra, S.; Dash, V.; Goyal, A.; Rath, G.
Comparative study of extraction, purification and estimation of bromelain from stem and fruit of pineapple plant
Thai J. Pharm. Sci.
34
67-76
2010
Ananas comosus
-
Arshad, Z.I.; Amid, A.; Yusof, F.; Jaswir, I.; Ahmad, K.; Loke, S.P.
Bromelain: an overview of industrial application and purification strategies
Appl. Microbiol. Biotechnol.
98
7283-7297
2014
Ananas comosus (O23791), Ananas comosus
Corzo, C.; Waliszewski, K.; Welti-Chanes, J.
Pineapple fruit bromelain affinity to different protein substrates
Food Chem.
133
631-635
2012
Ananas comosus (O23791)
Devi, Y.; Rupachandra Singh, L.; Kunjeshwori Devi, S.
Pineapple fruit bromelain and its application: A review
Indian J. Agric. Biochem.
25
1-7
2012
Ananas comosus (O23791)
-
Mohan, R.; Sivakumar, V.; Rangasamy, T.; Muralidharan, C.
Optimisation of bromelain enzyme extraction from pineapple (Ananas comosus) and application in process industry
Am. J. Biochem. Biotechnol.
12
188-195
2016
Ananas comosus (O23791)
-
Misran, E.; Idris, A.; Mat Sarip, S.; Yaakob, H.
Properties of bromelain extract from different parts of the pineapple variety Morris
Biocatal. Agricult. Biotechnol.
18
101095
2019
Ananas comosus
-
Ramli, A.N.M.; Manas, N.H.A.; Hamid, A.A.A.; Hamid, H.A.; Illias, R.M.
Comparative structural analysis of fruit and stem bromelain from Ananas comosus
Food Chem.
266
183-191
2018
Ananas comosus (O23791), Ananas comosus
Chakraborty, S.; Rao, P.; Mishra, H.
Modeling the inactivation kinetics of fruit bromelain in pineapple during high-pressure and thermal treatments
Innov. Food Sci. Emerg. Technol.
33
10-18
2016
Ananas comosus (O23791)
-
Sao Paulo Barretto Miranda, I.K.; Fontes Suzart Miranda, A.; Souza, F.V.; Vannier-Santos, M.A.; Pirovani, C.P.; Pepe, I.M.; Rodowanski, I.J.; Ferreira, K.T.; Mendes Souza Vaz, L.; de Assis, S.A.
The biochemical characterization, stabilization studies and the antiproliferative effect of bromelain against B16F10 murine melanoma cells
Int. J. Food Sci. Nutr.
68
442-454
2017
Ananas comosus (O23791), Ananas comosus (O23801), Ananas comosus AGB 772 (O23791), Ananas comosus AGB 772 (O23801)
Das, S.; Bhattacharyya, D.
Destabilization of human insulin fibrils by peptides of fruit bromelain derived from Ananas comosus (pineapple)
J. Cell. Biochem.
118
4881-4896
2017
Ananas comosus (O23791), Ananas comosus
Ghensi, P.; Cucchi, A.; Bonaccorso, A.; Ferroni, L.; Gardin, C.; Mortellaro, C.; Zavan, B.
In vitro effect of bromelain on the regenerative properties of mesenchymal stem cells
J. Craniofac. Surg.
30
1064-1067
2019
Ananas comosus (O24641)
Andjaitan, M.; Tutunnugrah, T.; Pamudja, K.; Idris, F.; Tjandra, M.; Wiriantono, T.
Bromelain enzyme from pineapple fruit as an antiviral agent against HIV, hepatitis C and human papiloma virus
J. Eng. Appl. Sci.
13
3125-3130
2018
Ananas comosus (O23791)
-
Zhi, N.; Zong, K.; Jia, X.; Wang, L.; Liang, J.
Effect of high pressure processing on fibrinolytic activity of fruit bromelain in vivo
J. Food Process Eng.
42
e13146
2019
Ananas comosus (O23791)
-
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