Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Louis P. Lessard"'
Publikováno v:
Biotechnology Progress. 19:1255-1260
The kinetics of esterification of conjugated linoleic acid (CLA) with sorbitol in acetone was investigated. An immobilized lipase from Candida antarctica (Chirazyme L-2) was used as the biocatalyst. A 2(2) x 3 factorial design was employed to find an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::267e83df3af6dabd5cbacaf5a83f2ce4
https://doi.org/10.1021/bp0340178
https://doi.org/10.1021/bp0340178
Publikováno v:
Biochemical Engineering Journal. 23:107-116
A 23 factorial design with a central point was utilized to develop a multi-response model of the kinetics of the transesterification reaction between menhaden oil and the ethyl ester of conjugated linoleic acid in the presence of an immobilized lipas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::35e409e8e11fea48d9045420ecb3eaa3
https://doi.org/10.1016/j.bej.2004.10.012
https://doi.org/10.1016/j.bej.2004.10.012
Publikováno v:
Journal of the American Oil Chemists' Society. 80:873-880
The kinetics of the interesterification reaction between menhaden oil and the ethyl ester of CLA (CLAEE) in the presence of an immobilized lipase from Rhizomucor miehei was investigated. A 23 factorial design with a central point was used to define t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::72cb30f1e4dc884e46d1109e7b80562f
https://doi.org/10.1007/s11746-003-0788-8
https://doi.org/10.1007/s11746-003-0788-8
Publikováno v:
Journal of the American Oil Chemists' Society. 79:655-661
Solvent-free acidolysis of tristearin with CLA has been carried out in a packed-bed reactor. An immobilized lipase from Thermomyces lanuginosa (Lipozyme TL IM) was employed as the biocatalyst. Elevated temperatures (75°C) were utilized to eliminate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f6ba4792b104473988a86c851709f42
https://doi.org/10.1007/s11746-002-0539-x
https://doi.org/10.1007/s11746-002-0539-x
Autor:
Louis P. Lessard, Charles G. Hill
Publikováno v:
Biotechnology and Bioengineering. 70:332-341
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::abecc6a7fd7c6e1ad7a4b96bc75aa45a
https://doi.org/10.1002/1097-0290(20001105)70:3<332::aid-bit10>3.0.co
https://doi.org/10.1002/1097-0290(20001105)70:3<332::aid-bit10>3.0.co
Autor:
Charles G. Hill, Louis P. Lessard
Publikováno v:
Biotechnology and Bioengineering. 69:183-195
The lipolysis of butter oil in a hollow-fiber reactor containing an immobilized calf pregastric esterase was studied at 40°C and at pH values of 4.0, 5.0, 6.0, and 7.0. The concentrations of ten fatty acid species in the lipolyzed product were deter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::685c59fc6b327a1cee0d60e65d425c5a
https://doi.org/10.1002/(sici)1097-0290(20000720)69:2<183::aid-bit7>3.0.co
https://doi.org/10.1002/(sici)1097-0290(20000720)69:2<183::aid-bit7>3.0.co
Publikováno v:
LWT - Food Science and Technology. 28:253-258
Lingual Upases from calf, lamb and goal were semi-purified by cold storage and microfiltralion, and subsequently immobilized by physical adsorption on hollow fibers fabricated of microporous polypropylene. The immobilized lipases were employed in a h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::88bf917afe73305b93e495320d8d6b10
https://doi.org/10.1016/s0023-6438(95)94035-9
https://doi.org/10.1016/s0023-6438(95)94035-9
Autor:
Charles G. Hill, Louis P. Lessard
Publikováno v:
Biotechnology and bioengineering. 79(3)
Lipolysis of butter oil in a hollow fiber reactor containing an immobilized calf pregastric esterase was studied at 40°C, a pH of 6.0, and glycerol concentrations of 0, 150, and 500 g/L in the buffer solution. The concentrations of 10 fatty acid spe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c7fc5006cb394c2dec197fcff6cb3e0
https://pubmed.ncbi.nlm.nih.gov/12115421
https://pubmed.ncbi.nlm.nih.gov/12115421