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Enzymatic Biocatalysis in Self-Assembled Media q
Gupte, A.; Nagarajan, R.; Kilara, A. Block
Copolymer Microdomains. A Novel Medium for Enzymatic Reactions, Biotechnology
Progress 7, 348-354 (1991). q
Gupte, A.; Nagarajan, R.; Kilara, A.
Enzymatic Oxidation of Cholesterol in Reverse Micelles, Industrial
and Engineering Chemistry Research 34, 2910-2922 (1995). q
Gupte, A.; Nagarajan, R.; Kilara, A. Enzyme
Reactions in Reverse Micelles. In FOOD FLAVORS: GENERATION, ANALYSIS AND
PROCESS INFLUENCE, Charalambous, G., (Ed.),
Elsevier, q
Patel, M. T.; Nagarajan, R.; Kilara, A. Characteristics of Lipase-Catalyzed Hydrolysis
of Triacylglycerols in Aerosol-OT/iso-octane Reverse Micellar Media. Biotechnology and
Applied Biochemistry 22, 1-14 (1995). q
Patel, M. T.; Nagarajan, R.; Kilara, A. Hydrolysis of Milk Fats by Commercial Lipases
in Solvent-free Phospholipid Reverse Micellar Media. Journal
of Food Science 61, 33-38 (1996). q
Patel, M. T.; Nagarajan, R.; Kilara, A. Interactive Influence and optimization of
Reaction Parameters in the Hydrolysis of Olive and Coconut Triacylglycerols by C. Cylindraceae
and R. Javanicus Lipases in Reverse Micellar Media.
Applied Biochemistry and Biotechnology 59, 109-124 (1996). q
Patel, M. T.; Nagarajan, R.; Kilara, A. Lipase-Catalyzed Biochemical Reactions in
Novel Media-A Review. Chemical Engineering Communications 152, 365-404
(1996). Related Graduate
Student Thesis Ø Gupte, Anagha
(Ph.D. 92) "Enzymatic Biocatalysts in Colloidal Media" (with A. Kilara) Ø
Patel, Mayank
(Food Science, Ph.D. 93) "Lipase Catalyzed Hydrolysis of Fats and Oils
in Reverse Micelle Systems" (with A.Kilara)
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Conversion of Cholesterol to Cholestenone Catalyzed by Cholesterol
Oxidase in Water-Poor Media |
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Conversion of cholesterol to cholestenone catalyzed by
cholesterol oxidase is carried out in PEO-PPO-PEO block copolymer
microdomains, which are generated spontaneously in the block copolymer
– cyclohexane – water system.
The reaction takes place with the enzyme located in the PEO rich
domains and the substrate and the product located in the PPO rich
domains. The coproduct hydrogen peroxide, which can inactivate the enzyme, is
removed as soon as it is produced by the action of
the enzyme catalase via a decomposition reaction. |
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The figure shows the measured percent relative activity
of cholesterol in block copolymer microdomains and in aqueous solution at 25oC,
as a function of time. The activity
is relative with respect to that at time zero when the enzyme is added to the
reaction mixture. The microdomain experiments are
those performed with a 16.7 volume
percent solution of the block copolymer Pluronic L61 in cyclohexane, with
water to the copolymer molar ratio of R = 7.1. The stability and activity of the enzyme in the block
copolymer system are even better than those in the aqueous medium. |
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Hydrolysis of Milk Triacylglycerols by R. Javanicus
Lipase in Solvent-Free Reverse Micellar Media. |
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Interactive effects
of reaction parameters on hydrolysis of milk triacylglycerols
by R. javanicus lipase in solvent-free reverse
micellar media. Reaction
parameters: phospholipid concentration 5 50 mM,
substrate concentration 5 94.5%, v/v, enzyme concentration 5 5 mg/10 mL. In the bottom figure, R stands for the
molar ratio of water to the phospholipid in the reverse micelle. |
