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SUMMARY:Fragment Based Active Site Exploration of Polyurethane Degrading E
 nzymes for Structure-guided Protein Engineering
DTSTART;VALUE=DATE-TIME:20250922T174000Z
DTEND;VALUE=DATE-TIME:20250922T175000Z
DTSTAMP;VALUE=DATE-TIME:20260526T072136Z
UID:indico-contribution-1866@lindico453.srv.lu.se
DESCRIPTION:Speakers: Deniz Bicer (Aarhus University)\nPolyurethane (PU) p
 lastics are extermyl durable and hard to recycle by convential methods due
  to\ncrosslinked and branched molecular structure. Recent discoveries of e
 nzyme that arget carbamate\n(urethane) bond in the PU provide alternative 
 way of PU recycling by means of biocatalytic degradation.\nEnZync center h
 as been established to discover\, characterize and engineer novel enzymes 
 for PU\ndegradation. So far we have discovered several enzymes by computat
 ional searches and experimental\nways. The critical steps to establish rat
 ional basis of protein engineering campaing is the understanding\nof Plast
 ic-enzyme interactions at molecular level. To pursue structural characteri
 zation of “PURases”\nwe have two different but complemantry methods to
  characteirze active site of PURases: i) Fragment\nBased Active site Explo
 ration (FASE) of PURases by using small molecule fragment libraries and\ns
 oluble PU analogs and ii) time-resolved serial crystallography by cryocapt
 uring catalytic intermideate\n(for slow-milisecond kinetics) and ambient t
 emperature (fast-microsecond) crystallography. We have\ncompleted FASE app
 roaches for one of our patented enzymes and now we are strating to perform
  serial\ncrystallography approach with promising preliminary data.\n\nAuth
 ors: Deniz Bicer\, Laura Rotilio\, Daniel Otzen & Jens Preben Morth\n\nhtt
 ps://lindico453.srv.lu.se/event/583/contributions/1866/
LOCATION:LINXS at The Loop
URL:https://lindico453.srv.lu.se/event/583/contributions/1866/
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