Proteomic characterization and antifungal activity of potato tuber proteins isolated from starch production waste under different temperature regimes
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12220%2F18%3A43897690" target="_blank" >RIV/60076658:12220/18:43897690 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00216224:14740/18:00106168
Výsledek na webu
<a href="http://dx.doi.org/10.1007/s00253-018-9373-y" target="_blank" >http://dx.doi.org/10.1007/s00253-018-9373-y</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s00253-018-9373-y" target="_blank" >10.1007/s00253-018-9373-y</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Proteomic characterization and antifungal activity of potato tuber proteins isolated from starch production waste under different temperature regimes
Popis výsledku v původním jazyce
Proteins were obtained from effluent of a starch manufacture by using different isolation temperatures (40, 60, 80, and 100 °C). The proteins, remaining in effluent after treatment of potato juice at 80 and 100 °C differed significantly in composition and in structural stability as well as in trypsin inhibitory and antifungal activities in comparison with the variants of 40 and 60 °C. The protein samples of 80 °C exhibited the highest antifungal activity and its average value of IC50 against five strains of two Fusarium species was determined in average at 0.18 mg ml−1. The 80 °C protein samples consisted predominantly of lowmolecular proteins (7–17 kDa) identified as potato tuber protease inhibitors I and II. Predominantly, protease inhibitors II were identified for the protein samples obtained by 100 °C and here we identified 7 spots in comparison with 12 identified for the 80 °C samples. Samples of 40 and 60 °C with low antifungal activities represent high variability of detected and identified proteins.We identified various representatives of aspartic, cysteine, and serine protease inhibitors in both types of samples. These samples also contained Kunitz-type protease inhibitors that were not found in the 80 and 100 °C samples which documented thermal unstableness of Kunitz-type protease inhibitors. Functional stability at high temperatures and antifungal activity of isolated potato protease inhibitors I and II support the potential of this fraction usage in food, feed, pharmaceutical, or agricultural industry and offer new products for starch manufactures. At the same time, utilization of the stable protein fraction of waste deproteinized potato water promotes exploitation of potato starch production resources.
Název v anglickém jazyce
Proteomic characterization and antifungal activity of potato tuber proteins isolated from starch production waste under different temperature regimes
Popis výsledku anglicky
Proteins were obtained from effluent of a starch manufacture by using different isolation temperatures (40, 60, 80, and 100 °C). The proteins, remaining in effluent after treatment of potato juice at 80 and 100 °C differed significantly in composition and in structural stability as well as in trypsin inhibitory and antifungal activities in comparison with the variants of 40 and 60 °C. The protein samples of 80 °C exhibited the highest antifungal activity and its average value of IC50 against five strains of two Fusarium species was determined in average at 0.18 mg ml−1. The 80 °C protein samples consisted predominantly of lowmolecular proteins (7–17 kDa) identified as potato tuber protease inhibitors I and II. Predominantly, protease inhibitors II were identified for the protein samples obtained by 100 °C and here we identified 7 spots in comparison with 12 identified for the 80 °C samples. Samples of 40 and 60 °C with low antifungal activities represent high variability of detected and identified proteins.We identified various representatives of aspartic, cysteine, and serine protease inhibitors in both types of samples. These samples also contained Kunitz-type protease inhibitors that were not found in the 80 and 100 °C samples which documented thermal unstableness of Kunitz-type protease inhibitors. Functional stability at high temperatures and antifungal activity of isolated potato protease inhibitors I and II support the potential of this fraction usage in food, feed, pharmaceutical, or agricultural industry and offer new products for starch manufactures. At the same time, utilization of the stable protein fraction of waste deproteinized potato water promotes exploitation of potato starch production resources.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
40106 - Agronomy, plant breeding and plant protection; (Agricultural biotechnology to be 4.4)
Návaznosti výsledku
Projekt
<a href="/cs/project/LM2015043" target="_blank" >LM2015043: Česká infrastruktura pro integrativní strukturní biologii</a><br>
Návaznosti
S - Specificky vyzkum na vysokych skolach
Ostatní
Rok uplatnění
2018
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Applied Microbiology and Biotechnology
ISSN
0175-7598
e-ISSN
—
Svazek periodika
102
Číslo periodika v rámci svazku
24
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
10
Strana od-do
10551-10560
Kód UT WoS článku
000451523800017
EID výsledku v databázi Scopus
2-s2.0-85054294321