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Information on EC 3.4.22.14 - actinidain and Organism(s) Actinidia deliciosa and UniProt Accession A5HII1
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3.4.22.14 actinidainSpecify your search results
Word Map
- 3.4.22.14
- papain
- kiwifruit
- proteinases
- allergen
-
kiwi
- deliciosa
-
catalytic-site
- hayward
- ficin
- bromelain
-
thaumatin-like
- chymopapains
-
hort16a
-
brocklehurst
-
cysteine-proteinase
- kiwellin
- medicine
-
two-protonic-state
-
active-centre
- synthesis
- food industry
- nutrition
- molecular biology
- biotechnology
The taxonomic range for the selected organisms is: Actinidia deliciosa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
actinidin, act d 1, actinidain, act1a-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
actinidia anionic protease
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-
-
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actinidin
mercaptoproteinase A2
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-
-
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proteinase A2 of Actinidia chinensis
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-
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actinidin
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY
39279-27-1
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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
amylase + H2O
?
human salivary amylase is highly susceptible to digestion with actinidin. 83% of amylase function is lost within a 5 minutes incubation period at 37°C in mixtures of 1 part kiwifruit: 3 parts saliva
-
-
?
Collagen type I + H2O
?
the hydrolysis of types I and II collagen by actinidin under different pH conditions is monitored by SDS-PAGE: good digestion of type I collagen at pH 7 (phosphate buffer) or pH 8.5 (Tris-HCl buffer). In citrate buffer (pH 5.5), actinidin digests more than half of the collagen type I, but in acetate buffer (pH 4), the enzyme does not hydrolyze this substrate
-
-
?
collagen type II + H2O
?
the hydrolysis of types I and II collagen by actinidin under different pH conditions is monitored by SDS-PAGE: good digestion of type I collagen at pH 7 (phosphate buffer) or pH 8.5 (Tris-HCl buffer). In citrate buffer (pH 5.5), or acetate buffer (pH 4), the enzyme does not hydrolyze this substrate
-
-
?
human occludin + H2O
?
human occludin is fragmented, and putative Act d1 cleavage sites are identified in extracellular loops of human occludin
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-
?
Collagen + H2O
?
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efficiently hydrolized at neutral or mild basic pH
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-
?
collagen type II + H2O
?
actinidin can hydrolyze collagen types I and II at neutral and alkaline pH
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-
?
Fibrinogen + H2O
?
-
efficiently hydrolized at neutral or mild basic pH
-
-
?
kiwellin + H2O
KiTH + kissper
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in vitro treatment of purified kiwellin, an allergenic protein formerly isolated from green kiwi fruit, with the protease actinidin from green kiwi fruit originates KiTH, a 20 kDa protein with 100% identity with the C-terminal region of kiwellin, and kissper, a described pore-forming peptide
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-
?
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester + H2O
N-alpha-benzyloxycarbonyl-L-lysine + 4-nitrophenol
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-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys 4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + 4-nitrophenol
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-
-
-
?
sheep IgG + H2O
?
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actinidin is ineffective on the heavy chain but has limited effects on the light chain
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-
?
Collagen type I + H2O
?
actinidin can hydrolyze collagen types I and II at neutral and alkaline pH
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-
?
Collagen type I + H2O
?
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actinidain cleaves between Gly1032 and Gly1033, limited hydrolysis by actinidain protease produces monomeric collagen, which consisted almost entirely of alpha1 and alpha2 chains
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-
?
atelocollagen + H2O
additional information
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-
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actinaidin cleaves the atelocollagen molecule at specific sites on the inside of the interstrand cross-linking peptides. The actinidain-processed atelocollagen shows only monomeric alpha1 and alpha2 chains, with no beta and gamma chains, atelocollagen retains its typical triple helical structure
?
additional information
?
-
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actinidin compared with type II or IV collagenase isolated from intact human umbilical vein endothelial cells, hepatocytes, and thymic epithelial cells with viability more than 90%
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-
?
additional information
?
-
actinidin compared with type II or IV collagenase isolated from intact human umbilical vein endothelial cells, hepatocytes, and thymic epithelial cells with viability more than 90%
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-
?
additional information
?
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-
digestibility of kiwifruit allergens, actinidin (Act d 1) and thaumatin-like protein (Act d 2), is assessed using an in vitro digestion system that approximates physiological conditions with respect to the passage of food through the stomach into the duodenum: Act d 1 precipitates in simulated gastric fluid at pH 2 and digestion of the aggregated protein proceeds slowly. The residual precipitate redissolves completely in simulated duodenal fluid at pH 6.5 and is partially digested. Act d 1 and Act d 2 display nearly unchanged IgE binding abilities
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?
additional information
?
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the SDSPAGE profile of cream milk treated with actinidin reveals that both caseins, whey proteins and MFGF proteins are sharply digested by the enzyme
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-
?
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
kiwellin + H2O
KiTH + kissper
-
in vitro treatment of purified kiwellin, an allergenic protein formerly isolated from green kiwi fruit, with the protease actinidin from green kiwi fruit originates KiTH, a 20 kDa protein with 100% identity with the C-terminal region of kiwellin, and kissper, a described pore-forming peptide
-
-
?
additional information
?
-
-
digestibility of kiwifruit allergens, actinidin (Act d 1) and thaumatin-like protein (Act d 2), is assessed using an in vitro digestion system that approximates physiological conditions with respect to the passage of food through the stomach into the duodenum: Act d 1 precipitates in simulated gastric fluid at pH 2 and digestion of the aggregated protein proceeds slowly. The residual precipitate redissolves completely in simulated duodenal fluid at pH 6.5 and is partially digested. Act d 1 and Act d 2 display nearly unchanged IgE binding abilities
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ba2+
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
Ca2+
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
Co2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
Fe2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
KCl
-
minimal activity at 0.5-0.8 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 0.8 M
LiCl
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minimal activity at 1.0-1.5 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 1.5 M
Mg2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
Mn2+
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addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
NaCl
-
minimal activity at 0.5-1.2 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 1.2 M
Zn2+
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
N-(trans-epoxysuccinyl)-L-leucine 4-guanidinobutylamide
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conformational mobility of actinidin changes upon binding of the inhibitor E-64, leading to a sequence of events that enables water and ions to protrude into a newly formed cavity of the inhibited enzyme
N-(trans-epoxysuccinyl)-L-leucine 4-guanidinobutylamide
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in contrast to actinidin without inhibitor, the actinidinE-64 complex starts degrading 15 min after incubation in simulated gastric fluid (SGF) and is fully degraded after 60 min of incubation. In addition transition maximum temperature (Tm) of the actinidin-inhibitor complex is 61°C in contrast to Tm: 73.9° of actinidin without inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-cysteine
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for activation of actinidin, 52 mM L-cysteine is added to the sample and the preparation incubated for 1 h at 45°C
L-cysteine
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the enzyme is activated in 20 mM potassium phosphate buffer, pH 6.5 containing 52 mM L-cysteine and 2 mM EDTA (1:1 (v/v)) for 1 h at 45°C
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0582
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester
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pH 6.5, 27°C, Vmax: 2.14 miroM/sec
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
42.8
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester
-
pH 6.5, 27°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
730
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester
-
pH 6.5, 27°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
actinidin is present in small cells, but not large cells in the outer pericarp of mature Actinidia deliciosa fruit at harvest. Within the small cells, actinidin is localised diffusely in the vacuole, associated with the plasma membrane, and in a layer in the plastids near starch granules
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actinidin mRNAs for acidic and basic proteins are expressed at comparable levels throughout ripening. Actinidin mRNA expression is highest in fruit at harvest, expression decreases as fruit ripened and is much lower in the core compared with outer pericarp tissue. Low levels of a basic actinidin protein (KFAct2a) in ripe Actinidia deliciosa fruit. Extremely high levels of an acidic actinidin protein (KFAct1a) is detected in Actinidia deliciosa fruit. Both the basic and acidic actinidin isoforms in Actinidia deliciosa are active cysteine proteases
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
actinidin is present in small cells, but not large cells in the outer pericarp of mature Actinidia deliciosa fruit at harvest. Within the small cells, actinidin is localised diffusely in the vacuole, associated with the plasma membrane, and in a layer in the plastids near starch granules
-
actinidin is present in small cells, but not large cells in the outer pericarp of mature Actinidia deliciosa fruit at harvest. Within the small cells, actinidin is localised diffusely in the vacuole, associated with the plasma membrane, and in a layer in the plastids near starch granules
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
active actinidin retains its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion
physiological function
additional information
physiological function
-
actinidin disrupts the epithelial barrier function of human intestinal T84 cells by degrading the tight junction protein occludin. Exposure of T84 cells to biologically active actinidin significantly decreases the transepithelial resistance across the intestinal epithelial monolayers
physiological function
-
actinidin is both immunogenic and allergenic at relatively low doses. Vigorous IgG and IgG1 antibody and high titre IgE antibody responses are recorded in response to actinidin
additional information
the enzyme increases intestinal permeability in both in vivo (mice) and in vitro (Caco-2 cell culture) models. The food allergen with intrinsic proteolytic activity can compromise the gut epithelial barrier, contributing to the sensitization process in food allergy pathogenesis
additional information
-
the enzyme increases intestinal permeability in both in vivo (mice) and in vitro (Caco-2 cell culture) models. The food allergen with intrinsic proteolytic activity can compromise the gut epithelial barrier, contributing to the sensitization process in food allergy pathogenesis
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). ACTN_ACTDE
380
1
42110
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P75Q
-
the mutant shows reduced activity compared tot he wild type enzyme
S68G/P75Q
-
the mutant shows reduced activity compared tot he wild type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 12
-
immobilized actinidin is more stable than free form at pH 3 and pH 12 after 60 min incubation leading to 30% residual activity of immobilized form and complete inactivation of the free form
733988
additional information
-
thermal stability of Act d 1 and Act d 2 is strongly pH dependent. Act d 1 is irreversibly destabilized in acidic solutions (pH 3.5)
700290
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
active actinidin retains its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, 30 days, free actinidin shows no activity while immobilized actinidin shows 90% activity
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4°C, 60 days, free actinidin shows no activity while immobilized actinidin shows 80% activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the enzyme fraction is precipitated from kiwifruit extract by 60% saturation of ammonium sulfate. The precipitate is redissolved in 50 mM citrate buffer (pH 5.5) and dialyzed overnight against this buffer. The dialyzate is loaded into a DEAE-Sepharose Fast Flow column, which pre-equilibrated with the same buffer. The adsorbed fractions are eluted with 0.0-1 M linear gradient of sodium chloride in the buffer
Act d 1 is purified from kiwifruit extracts by covalent chromatography using activated thiopropyl sepharose 6B
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Actinidin is purified from the soluble fraction of kiwi fruit by ion exchange chromatography on DE-52 and Mono-Q columns
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DEAE-Sephadex A-50 gel filtration and SP-Sephadex C-50 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
medicine
the enzyme increases intestinal permeability in both in vivo (mice) and in vitro (Caco-2 cell culture) models. The food allergen with intrinsic proteolytic activity can compromise the gut epithelial barrier, contributing to the sensitization process in food allergy pathogenesis
molecular biology
actinidin compared with type II or IV collagenase isolates intact human umbilical vein endothelial cells, hepatocytes, and thymic epithelial cells with viability more than 90%
biotechnology
-
actinidin might be utilized to eliminate the milk fat globule membranes (MFGM) protein residues from cream and its derivatives
medicine
nutrition
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actinidin induces protease-dependent morphology changes of T84 human colorectal adenocarcinoma cells leading to cell rounding and desquamation of the epithelial monolayer, without affecting cell viability
synthesis
the enzyme can be used efficiently for hydrolysis of collagen and isolation of different cell populations from various solid tissues
food industry
actinidin, particularly at level 20 unit/g of skin, can be used to improve the yield and properties of gelatin from bovine skin
medicine
-
to isolate major kiwifruit allergens a large group of kiwi-sensitized patients with different clinical symptoms are investigated. The three major IgE-binding proteins from kiwifruit extracts are isolated and characterized. The isolated kiwifruit allergens are: actinidin Act d 1, glycosylated thaumatin-like Act d 2 and a novel 40 kDa glycoprotein designated as Act d 3.02. Specific IgE to each of the three allergens is found in over 60% of sera from kiwi-sensitized patients, and Act d 1 and Act d 2 induces positive SPT responses in over 50% of the tested patients. A significant link between IgE levels to Act d 1 and Act d 3 and anaphylaxis is uncovered. Act d 1, Act d 2 and Act d 3 are major allergens in the population studied. Severe symptoms after kiwi ingestion are associated with high IgE levels to Act d 1 and Act d 3
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morimoto, K.; Kunii, S.; Hamano, K.; Tonomura, B.
Preparation and structural analysis of actinidain-processed atelocollagen of yellowfin tuna (Thunnus albacares)
Biosci. Biotechnol. Biochem.
68
861-867
2004
Actinidia deliciosa
Morimoto, K.; Furuta, E.; Hashimoto, H.; Inouye, K.
Effects of high concentration of salts on the esterase activity and structure of a kiwifruit peptidase, actinidain
J. Biochem.
139
1065-1071
2006
Actinidia deliciosa
Mostafaie, A.; Bidmeshkipour, A.; Shirvani, Z.; Mansouri, K.; Chalabi, M.
Kiwifruit actinidin: a proper new collagenase for isolation of cells from different tissues
Appl. Biochem. Biotechnol.
144
123-131
2008
Actinidia deliciosa, Actinidia deliciosa (A5HII1)
Lucas, J.S.; Nieuwenhuizen, N.J.; Atkinson, R.G.; Macrae, E.A.; Cochrane, S.A.; Warner, J.O.; Hourihane, J.O.
Kiwifruit allergy: actinidin is not a major allergen in the United Kingdom
Clin. Exp. Allergy
37
1340-1348
2007
Actinidia deliciosa
Nieuwenhuizen, N.J.; Beuning, L.L.; Sutherland, P.W.; Sharma, N.N.; Cooney, J.M.; Bieleski, L.R.; Schroeder, R.; MacRae, E.A.; Atkinson, R.G.
Identification and characterisation of acidic and novel basic forms of actinidin, the highly abundant cysteine protease from kiwifruit
Funct. Plant Biol.
34
946-961
2007
Actinidia chinensis, Actinidia deliciosa
Palacin, A.; Rodriguez, J.; Blanco, C.; Lopez-Torrejon, G.; Sanchez-Monge, R.; Varela, J.; Jimenez, M.A.; Cumplido, J.; Carrillo, T.; Crespo, J.F.; Salcedo, G.
Immunoglobulin E recognition patterns to purified Kiwifruit (Actinidinia deliciosa) allergens in patients sensitized to Kiwi with different clinical symptoms
Clin. Exp. Allergy
38
1220-1228
2008
Actinidia deliciosa
Tuppo, L.; Giangrieco, I.; Palazzo, P.; Bernardi, M.L.; Scala, E.; Carratore, V.; Tamburrini, M.; Mari, A.; Ciardiello, M.A.
Kiwellin, a modular protein from green and gold kiwi fruits: evidence of in vivo and in vitro processing and IgE binding
J. Agric. Food Chem.
56
3812-3817
2008
Actinidia deliciosa
Bublin, M.; Radauer, C.; Knulst, A.; Wagner, S.; Scheiner, O.; Mackie, A.R.; Mills, E.N.; Breiteneder, H.
Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein
Mol. Nutr. Food Res.
52
1130-1139
2008
Actinidia deliciosa
Morimoto, K.; Kawabata, K.; Kunii, S.; Hamano, K.; Saito, T.; Tonomura, B.
Characterization of type I collagen fibril formation using thioflavin T fluorescent dye
J. Biochem.
145
677-684
2009
Actinidia deliciosa
Kunii, S.; Morimoto, K.; Nagai, K.; Saito, T.; Sato, K.; Tonomura, B.
Actinidain-hydrolyzed type I collagen reveals a crucial amino acid sequence in fibril formation
J. Biol. Chem.
285
17465-17470
2010
Actinidia deliciosa
Grozdanovic, M.; Popovic, M.; Polovic, N.; Burazer, L.; Vuckovic, O.; Atanaskovic-Markovic, M.; Lindner, B.; Petersen, A.; Gavrovic-Jankulovic, M.
Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy
Food Chem. Toxicol.
50
1013-1018
2012
Actinidia deliciosa
Cavic, M.; Grozdanovic, M.; Bajic, A.; Srdic-Rajic, T.; Andus, P.R.; Gavrovic-Jankulovic, M.
Actinidin, a protease from kiwifruit, induces changes in morphology and adhesion of T84 intestinal epithelial cells
Phytochemistry
77
46-52
2012
Actinidia deliciosa
Nieuwenhuizen, N.J.; Maddumage, R.; Tsang, G.K.; Fraser, L.G.; Cooney, J.M.; De Silva, H.N.; Green, S.; Richardson, K.A.; Atkinson, R.G.
Mapping, complementation, and targets of the cysteine protease actinidin in kiwifruit
Plant Physiol.
158
376-388
2012
Actinidia chinensis, Actinidia deliciosa
Chalabi, M.; Khademi, F.; Yarani, R.; Mostafaie, A.
Proteolytic activities of kiwifruit actinidin (Actinidia deliciosa cv. Hayward) on different fibrous and globular proteins: a comparative study of actinidin with papain
Appl. Biochem. Biotechnol.
172
4025-4037
2014
Actinidia deliciosa, Actinidia deliciosa cv. Hayward
Grozdanovic, M.M.; Drakulic, B.J.; Gavrovic-Jankulovic, M.
Conformational mobility of active and E-64-inhibited actinidin
Biochim. Biophys. Acta
1830
4790-4799
2013
Actinidia deliciosa
Puglisi, I.; Petrone, G.; Lo Piero, A.
A kiwi juice aqueous solution as coagulant of bovine milk and its potential in Mozzarella cheese manufacture
Food Bioprod. Process.
92
67-72
2014
Actinidia deliciosa
-
Cavic, M.; Grozdanovic, M.M.; Bajic, A.; Jankovic, R.; Andjus, P.R.; Gavrovic-Jankulovic, M.
The effect of kiwifruit (Actinidia deliciosa) cysteine protease actinidin on the occludin tight junction network in T84 intestinal epithelial cells
Food Chem. Toxicol.
72
61-68
2014
Actinidia deliciosa
Homaei, A.; Etemadipour, R.
Improving the activity and stability of actinidin by immobilization on gold nanorods
Int. J. Biol. Macromol.
72
1176-1181
2015
Actinidia deliciosa
Dearman, R.J.; Beresford, L.; Foster, E.S.; McClain, S.; Kimber, I.
Characterization of the allergenic potential of proteins: an assessment of the kiwifruit allergen actinidin
J. Appl. Toxicol.
34
489-497
2014
Actinidia deliciosa
Grozdanovic, M.M.; Ostojic, S.; Aleksic, I.; Andjelkovic, U.; Petersen, A.; Gavrovic-Jankulovic, M.
Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart
J. Sci. Food Agric.
94
3046-3052
2014
Actinidia deliciosa
Grozdanovic, M.M.; Cavic, M.; Nesic, A.; Andjelkovic, U.; Akbari, P.; Smit, J.J.; Gavrovic-Jankulovic, M.
Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions
Biochim. Biophys. Acta
1860
516-526
2016
Actinidia deliciosa (A5HII1), Actinidia deliciosa
Martin, H.; Cordiner, S.B.; McGhie, T.K.
Kiwifruit actinidin digests salivary amylase but not gastric lipase
Food Funct.
8
3339-3345
2017
Actinidia deliciosa (A5HII1), Actinidia deliciosa
Ahmad, T.; Ismail, A.; Ahmad, S.; Khalil, K.; Teik Kee, L.; Awad, E.; Sazili, A.
Physicochemical characteristics and molecular structures of gelatin extracted from bovine skin effects of actinidin and papain enzymes pretreatment
Int. J. Food Prop.
22
138-153
2019
Actinidia deliciosa (A5HII1)
-
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