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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