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UID:1242@biotech.technion.ac.il
DTSTART;TZID=Asia/Jerusalem:20261021T140000
DTEND;TZID=Asia/Jerusalem:20261021T150000
DTSTAMP:20261004T111008Z
URL:https://biotech.technion.ac.il/events/%d7%a1%d7%9e%d7%99%d7%a0%d7%a8-%
 d7%a1%d7%99%d7%95%d7%9d-%d7%93%d7%95%d7%a7%d7%98%d7%95%d7%a8%d7%98-%d7%a4%
 d7%96-%d7%a9%d7%9e%d7%a9-%d7%9e%d7%94%d7%9e%d7%a2%d7%91%d7%93%d7%94-%d7%a9
 %d7%9c-%d7%a4/
SUMMARY:סמינר סיום דוקטורט: פז שמש\, מהמעבדה ש
 ל פרופ' אילת פישמן
DESCRIPTION:Research Topic: Characterization of rapeseed napin and potato p
 atatin proteins expressed and produced from Pichia pastoris\nAbstract: ** 
 Lecture will be given in English**\nCan plant proteins be produced without
  extracting them from the plant\, while preserving the properties that mak
 e them useful food ingredients? Direct extraction is influenced by growth 
 conditions\, raw-material composition\, and the presence of antinutritiona
 l compounds\, while processing itself may alter protein properties. This s
 tudy explores an alternative: recombinant plant protein production using P
 ichia pastoris under controlled fermentation conditions.\nThe work began w
 ith development of a fermentation platform. Different P. pastoris strains\
 , carbon sources\, and cultivation conditions were evaluated\, reaching mo
 re than 240 g/L dry cell weight under optimized conditions. Ploidy was als
 o examined using a fluorescent model protein\, revealing higher recombinan
 t protein production in diploid vs. haploid strains. The platform was then
  applied to two plant proteins: rapeseed napin and potato patatin. For nap
 in\, constitutive expression combined with a diploid strain resulted in ap
 proximately 8.8 g/L protein\, whereas for patatin\, methanol-induced expre
 ssion was more effective for production of the secreted protein. A diploid
  advantage was also observed for patatin.\nFollowing membrane-based concen
 tration and purification\, the recombinant proteins were compared with pla
 nt-derived counterparts. Recombinant napin showed a greater tendency to ag
 gregate while retaining high emulsifying activity under acidic conditions.
  In patatin\, the expression route affected both structure and function: t
 he secreted protein was glycosylated and showed higher emulsifying activit
 y\, whereas the intracellular form formed gels at lower concentrations.\nF
 inally\, secreted patatin was evaluated for emulsifying\, foaming\, and ge
 lation properties and incorporated into mayonnaise-type emulsions and gela
 tin-free gummies. Together\, these results connect fermentation strategy w
 ith protein properties and\, ultimately\, with performance in food applica
 tions.
CATEGORIES:סמינרים
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