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Kinetics of catalytic vapor phase esterificationHundley, John Gower, January 1953 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1953. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Bibliography: leaves 79-80.
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Kinetics of catalytic vapor phase esterificationSamsel, Claude Millard. January 1960 (has links)
Thesis (M.S.)--University of Wisconsin--Madison, 1960. / Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaf 63).
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Kinetics of catalytic vapor phase esterificationFricke, Arthur L. January 1962 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1962. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 124-127).
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Phase-transfer kinetics of esterification using crown ethers as phase-transfer agents.January 1980 (has links)
by Alex Wai Pui-Wah. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1980. / Bibliography: leaves 67-71.
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Kinetic studies in vapor phase esterification /Fitz, Richard Albert January 1956 (has links)
No description available.
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Studies of the Mechanism of Plasma Cholesterol Esterification in Aged RatsLee, Sun Min 12 1900 (has links)
The study was performed to determine factors influencing the esteriflcation of plasma cholesterol in young and aged rats. The distribution of LCAT activity was determined following gel nitration chromatography and ultracentrifugation of whole plasma respectively. When rat plasma was fractionated on a Bio-Gel A-5 Mcolumn, LCAT activity was found to be associated with the HDL fraction. A similar result was observed upon 24 hr density gradient ultracentrifugation of the plasma. However, following prolonged 40 hr preparative ultracentrifugation, the majority of the LCAT activity was displaced into the lipoprotein-free infranatant fraction (d> 1.225 g/ml). The dissociation of LCAT from the HDL fraction occured to a smaller extent in aged rat plasma than in young rat plasma. Plasma incubation (37°C) experiments followed by the isolation of lipoproteins and the subsequent analysis of their cholesterol content revealed that in vitro net esteriflcation of free cholesterol (FC) by LCAT as well as the fractional ufilization of HDL-FC as substrate were lower in the plasma of the aged animal as compared to that of the young animal despite the fact that the total pool of FC was higher in the former. The net transfer of FC from lower density lipoproteins (d<1.07 g/ml) to HDL provided the FC (in addition to HDL-FC) for esteriflcation in the plasma of both young and aged rats, and this process was not substantially affected by aging. Substrate specificity studies indicated that HDL from young rats was a better substrate for LCAT than the HDL from aged rats. The HDL isolated from the plasma of aged rats was enriched with apo E and had a considerably higher molecular weight than the HDL from young rat plasma. The ratio of phosphatidyl choline/sphingomyelin was lower in the HDL of aged rats. These data suggest that the decreased plasma cholesterol esteriflcation in aged rats is due to changes in the composition and size of the lipoprotein substrate (HDL).
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The reactivities of ionpair and free ion as the nucleophiles in solid-liquid phase transfer SN reaction catalyzed by crown ethers.January 1982 (has links)
by Ho-ming Leung. / Thesis (M. Phil.)--Chinese University of Hong Kong, 1982. / Bibliography: l. 63-67.
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Interesterification of butter fat by commercial microbial lipases in organic solvent mediaSafari, Mohammad January 1994 (has links)
The interesterification yield (IY) and changes in fatty acid positional distribution of selected butter fat triacylglycerols were investigated, using a wide range of commercial microbial lipases and organic solvent media. The interesterification of butter fat by lipase from Mucor miehei was carried out in hexane, hexane-chloroform, and hexane-ethyl acetate; the results showed that the addition of 30% of either chloroform or ethyl acetate to the hexane resulted in a 23% increase in the IY. The interesterification of butter fat in a microemulsion co-surfactant system, containing Brij 35 as surfactant and 1-heptanol as co-surfactant, resulted in an increase in the triacylglycerols that contain C18:0 at sn-2 position, located originally at sn-1,3 positions, with a concomitant interchange with C14:0 and C18:1 at the same position. The interesterification of butter fat by lipase from Rhizopus niveus, in a phosphatidylcholine reverse micellar system, showed an increase in C16:0 at the sn-2 position, with a concomitant decrease in the proportion of small chain fatty acids (C4-C10:0); however, the interesterification of butter fat in co-surfactant free microemulsion systems, containing hexane and ionic (phosphatidylcholine) and non-ionic (sorbitol monostearate and polyoxyethylene sorbitan monostearate) surfactants, showed that the interesterified selected triacylglycerols were enriched with C18:0 and C18:1, originally located on sn-1,3 position, at sn-2 position with concomitant interchange with C12:0, C14:0 and C16:0, originally located at the same position. The interesterification of butter fats, in co-surfactant free microemulsion system, by four microbial lipases showed that those catalyzed by lipase from R. niveus demonstrated a 46% increase in the proportion of C18:1 at sn-2 position whereas those catalyzed by enzymes from M. javanicus, R. delemar and M. miehei were enriched with C16:0 at the same position, by 21%, 35% and 41%, respectively. In addition, lipase from
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Production, purification, characterization of selected microbial lipases and their application for interesterification of butter fatPabai, Franknel Sandi Kouvea. January 1997 (has links)
The screening, biomass production of lipase-producing microorganisms from several sources, as well as the purification, characterization and utilization of the enzymatic extracts for the interesterification of butter fat were investigated. Pseudomonas fragi CRDA 323 and Aspergillus niger CBS 131.52 were considered to be good lipase producers, whereas, those from Pseudomonas putida ATCC 795 and Rhizopus oryzae ATCC 34612 as weak ones; all four microorganisms produced maximal amount of extracellular lipases by batch fermentation after three-four days of incubation in a continuously stirred tank reactor. The lipases were partially purified by ammonium sulfate precipitation and characterized with respect to pH, kinetic parameters and molecular size. The lipases from P. fragi and P. putida were optimal at pH 8.5 and 8.0, respectively, whereas those from A. niger and R. oryzae were optimal at pH 7.5. The A. niger lipase had the lowest V$ sb{max}$ value $ rm(0.51 times 10 sp3 U min sp{-1});$ R. oryzae the highest $ rm (1.86 times 10 sp3 U min sp{-1}).$ The K$ sb{m}$ values for P. fragi, P. putida, A. niger and R. oryzae lipases were 0.70, 1.18, 0.97 and 0.98 mg ml$ sp{-1},$ respectively. Interesterification of butter fat by the partially purified enzymatic extracts in a microemulsion free co-surfactant system containing sorbitol monostearate and polyoxyethylene sorbitan monostearate in the ratio 48:52 (V/V) decreased the water activity as well as the hydrolytic activity. The P. fragi lipase had the highest interesterification yield value (43%) and the R. oryzae lipase the lowest (4%). In addition, P. fragi lipase exhibited the highest decrease (18%) in long-chain hypercholesterolemic fatty acids (C12:0, C14:0 and C16:0) at the sn-2-position; the P. putida lipase demonstrated the least favorable changes in specificity at the same position. Continuous cultivation technique was developed to investigate the screening for lipase-producing microorganisms from four commercial
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Studies on the enzymatic esterification of phenols with sulfateBrunngraber, Eric G., January 1957 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1957. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves [80]-82).
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