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0344144935
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note
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12 or on the large scale more conveniently by transfer dehydrogenation with acetone, using Zn(II)/Sn(II) as catalysts.
-
-
-
-
66
-
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0345007368
-
-
note
-
-1 in 0.1 or 0.2 M metaphosphate buffer, pH 7, containing 20 mM calcium acetate, 5 °C), at an applied protein load of 10% w/w of PHOMS, gave the following activity immobilizations: papain, 96%; thermolysin, >99%; almond β-D-glucosidase, 98%; C. rugosa lipase-B, >99%; S. chromofuscus phospholipase D, 98%. Adsorption took 10-30 min, and less than 3% leaching of protein/activity was detected upon washing (3 × 10-fold volumes of buffer, 5 °C, 1 h).
-
-
-
-
67
-
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0344144934
-
-
note
-
-1.
-
-
-
-
68
-
-
0344576344
-
-
note
-
The silanol content of PHOMS varied between 6 and 12.3 mmol/g (46-93% of theoretical maximum), depending upon the mode of preparation and the aging and drying conditions. Wet processing at low pH and/or high temperature, and/or dry calcination affords a low-silanol/high-siloxane PHOMS. Conversely, low temperature and/or high pH treatment afford highly silanolated products. Silanol coverage was determined by titration with LAH, thermogravimetric analysis (TGA) and differential scanning calorimetry (DSC).
-
-
-
-
69
-
-
0345438440
-
-
note
-
18 This condensation is catalyzed by Sn(II), Fe(III), Ti(IV), Zn(II), Pt(IV), and other metal salts.
-
-
-
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70
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0012051982
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Silicon-Based Polymer Science: A Comprehensive Resource
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0344576343
-
-
note
-
It was calculated that C. rugosa lipase constituted less than 1% w/w of the total protein content of the crude enzyme preparation. Crude C. rugosa enzyme contains a number of lipase components. The adsorption of total lipolytic activity was followed, and no attempt was made to profile the adsorption of the various lipase species.
-
-
-
-
73
-
-
0344144933
-
-
note
-
-1.
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0345438436
-
-
note
-
-1 were exposed to 12 cycles of washing (15-30 mL of 50 mM phosphate, pH 7, containing 5% v/v 2-propanol, 15-20 h). 4-NPB hydrolysis and Lowry assays indicated that 6, 12, 13, 9, and 16% of lipase activity was desorbed respectively and that the adsorbates retained 91, 80, 83, 87, and 77% of their initial activities.
-
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77
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0030570083
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note
-
Titration with lithium aluminum hydride indicated that the silanol functionality available for cross-linking was reduced by 13-21% upon protein adsorption.
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note
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We have routinely fabricated lipase-PHOMS-silicone catalysts on a multikilo scale, and have estimated the costs of producing monoliths, granulates, coated particulates, and foams to be in the range of $20-35 per kilo of composite. The prices of commercial food and catalyst grade lipases range over $100-2000 per kilo. For medium to high catalytic density immobilizates (5-15% w/w lipase loading), the additional cost of immobilization is about 9-30%. Considering that the activities and long-term stabilities of the composites can exceed those of the native enzymes by 1-50-fold and 10-30-fold respectively, leading to performance improvements of 10-1500-fold, it can be seen that the economics are rather attractive.
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