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UID:1179@biotech.technion.ac.il
DTSTART;TZID=Asia/Jerusalem:20260706T140000
DTEND;TZID=Asia/Jerusalem:20260706T150000
DTSTAMP:20260630T095810Z
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%92%
 d7%99%d7%a0%d7%92-%d7%92%d7%99%d7%a0%d7%92-%d7%92%d7%90%d7%95-%d7%9e%d7%94
 %d7%9e%d7%a2/
SUMMARY:סמינר סיום דוקטורט: ג'ינג ג'ינג ג'או\, 
 מהמעבדה של פרופ' דגנית דנינו ופרופ' הרולד
  קורק
DESCRIPTION:Isolation and structural characterization of amylopectin cluste
 rs from waxy rice starch and their applications in functional complex desi
 gn\nAbstract: ** Lecture will be given in English**\nStarch\, as the prima
 ry component of our daily staples\, exhibits digestion characteristics tha
 t directly affect our blood sugar levels and overall health. Amylopectin i
 s the major component of starch\, accounting for approximately 65-85% of i
 ts total content. It is considered that the amylopectin primary limiting f
 actor during enzymatic hydrolysis. However\, due to its structural complex
 ity\, the precise mechanism by which amylopectin influences enzymatic dige
 stion remains to be fully elucidated.\nIn this study\, waxy rice starch (&
 gt\;99% amylopectin) was hydrolyzed using α-amylase (from Bacillus amylol
 iquefaciens) over varying durations to determine the reaction plateau. The
  hydrolysates at different time points were successfully isolated via anti
 -solvent precipitation. Systematic characterization and in vitro digestion
  assays revealed a highly branched "core" within the amylopectin structure
  that strongly resists further enzymatic cleavage\, which we defined as th
 e amylopectin cluster (APC).\nCharacterized by its highly branched nature 
 and short chain lengths\, the APC exhibits slow-digestion properties\, hig
 hlighting its potential as a prebiotic material. To further explore its fu
 nctional capabilities\, the APC was complexed with lauric acid (LA) and ca
 ffeic acid (CA). Results demonstrated that the APC successfully formed com
 plexes with both LA and CA\, driven primarily by hydrophobic interactions 
 and hydrogen bonding. The APC-LA complex exhibited increased slowly digest
 ible starch (SDS) content\, enhanced thermal stability\, and improved hydr
 ophobicity\, suggesting its potential as a Pickering emulsion stabilizer. 
 Furthermore\, the APC-CA complex significantly increased the total yield o
 f SDS and resistant starch (RS)\, while remarkably enhancing the antioxida
 nt stability of CA.\nOverall\, this study successfully isolated and elucid
 ated the inhibitory effect of amylopectin structural clusters on enzymatic
  hydrolysis\, offering a novel strategy for using these clusters to develo
 p digestion-resistant functional food complexes.
CATEGORIES:סמינרים
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DTSTART:20260327T030000
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