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Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart

Samo za registrovane korisnike
2014
Autori
Grozdanović, Milica
Ostojić, Sanja
Aleksić, Ivana
Anđelković, Uroš
Petersen, Arnd
Gavrović-Jankulović, Marija
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentu
Apstrakt
BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the tw...o actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry

Ključne reči:
actinidin / kiwi fruit / digestion / stability / E-64
Izvor:
Journal of the Science of Food and Agriculture, 2014, 94, 14, 3046-3052
Izdavač:
  • Wiley, Hoboken
Finansiranje / projekti:
  • Alergeni, antitela, enzimi i mali fiziološki značajni molekuli: dizajn, struktura, funkcija i značaj (RS-172049)

DOI: 10.1002/jsfa.6656

ISSN: 0022-5142

PubMed: 24633720

WoS: 000342829800029

Scopus: 2-s2.0-84917691939
[ Google Scholar ]
16
11
URI
http://intor.torlakinstitut.com/handle/123456789/411
Kolekcije
  • Radovi istraživača / Researchers’ publications
Institucija/grupa
Torlak
TY  - JOUR
AU  - Grozdanović, Milica
AU  - Ostojić, Sanja
AU  - Aleksić, Ivana
AU  - Anđelković, Uroš
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - http://intor.torlakinstitut.com/handle/123456789/411
AB  - BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry
PB  - Wiley, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart
EP  - 3052
IS  - 14
SP  - 3046
VL  - 94
DO  - 10.1002/jsfa.6656
UR  - conv_342
ER  - 
@article{
author = "Grozdanović, Milica and Ostojić, Sanja and Aleksić, Ivana and Anđelković, Uroš and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2014",
abstract = "BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry",
publisher = "Wiley, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart",
pages = "3052-3046",
number = "14",
volume = "94",
doi = "10.1002/jsfa.6656",
url = "conv_342"
}
Grozdanović, M., Ostojić, S., Aleksić, I., Anđelković, U., Petersen, A.,& Gavrović-Jankulović, M.. (2014). Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart. in Journal of the Science of Food and Agriculture
Wiley, Hoboken., 94(14), 3046-3052.
https://doi.org/10.1002/jsfa.6656
conv_342
Grozdanović M, Ostojić S, Aleksić I, Anđelković U, Petersen A, Gavrović-Jankulović M. Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart. in Journal of the Science of Food and Agriculture. 2014;94(14):3046-3052.
doi:10.1002/jsfa.6656
conv_342 .
Grozdanović, Milica, Ostojić, Sanja, Aleksić, Ivana, Anđelković, Uroš, Petersen, Arnd, Gavrović-Jankulović, Marija, "Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart" in Journal of the Science of Food and Agriculture, 94, no. 14 (2014):3046-3052,
https://doi.org/10.1002/jsfa.6656 .,
conv_342 .

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