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|a pubmed24n0560.xml
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|a (DE-627)NLM167860771
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|a (NLM)17241062
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Chen, Bo
|e verfasserin
|4 aut
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|a Effects of macroporous resin size on Candida antarctica lipase B adsorption, fraction of active molecules, and catalytic activity for polyester synthesis
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|c 2007
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Completed 28.02.2007
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|a Date Revised 24.11.2016
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|a published: Print
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|a Citation Status MEDLINE
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|a Methyl methacrylate resins with identical average pore diameter (250 A) and surface area (500 m2/g) but with varied particle size (35 to 560-710 microm) were employed to study how immobilization resin particle size influences Candida antarctica Lipase B (CALB) loading, fraction of active sites, and catalytic properties for polyester synthesis. CALB adsorbed more rapidly on smaller beads. Saturation occurred in less than 30 s and 48 h for beads with diameters 35 and 560-710 microm, respectively. Linearization of adsorption isotherm data by the Scatchard analysis showed for the 35 microm resin that: (i) CALB loading at saturation was well below that required to form a monolayer and fully cover the support surface and (ii) CALB has a high affinity for this resin surface. Infrared microspectroscopy showed that CALB forms protein loading fronts for resins with particle sizes 560-710 and 120 microm. In contrast, CALB appears evenly distributed throughout 35 microm resins. By titration with p-nitrophenyl n-hexyl phosphate (MNPHP), the fraction of active CALB molecules adsorbed onto resins was <50% which was not influenced by particle size. The fraction of active CALB molecules on the 35 microm support increased from 30 to 43% as enzyme loading was increased from 0.9 to 5.7% (w/w) leading to increased activity for epsilon-caprolactone (epsilon-CL) ring-opening polymerization. At about 5% w/w CALB loading, by decreasing the immobilization support diameter from 560-710 to 120, 75, and 35 microm, conversion of epsilon-CL % to polyester increased (20 to 36, 42, and 61%, respectively, at 80 min). Similar trends were observed for condensation polymerizations between 1,8-octanediol and adipic acid
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Enzymes, Immobilized
|2 NLM
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|a Fungal Proteins
|2 NLM
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|a Polyesters
|2 NLM
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|a Resins, Synthetic
|2 NLM
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|a Lipase
|2 NLM
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|a EC 3.1.1.3
|2 NLM
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|a lipase B, Candida antarctica
|2 NLM
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|a EC 3.1.1.3
|2 NLM
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|a Miller, Elizabeth M
|e verfasserin
|4 aut
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|a Miller, Lisa
|e verfasserin
|4 aut
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|a Maikner, John J
|e verfasserin
|4 aut
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|a Gross, Richard A
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 23(2007), 3 vom: 30. Jan., Seite 1381-7
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:23
|g year:2007
|g number:3
|g day:30
|g month:01
|g pages:1381-7
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_NLM
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|a GBV_ILN_22
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|a GBV_ILN_350
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|a GBV_ILN_721
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|a AR
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|d 23
|j 2007
|e 3
|b 30
|c 01
|h 1381-7
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