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Melek Tüter

Researcher at Istanbul Technical University

Publications -  30
Citations -  746

Melek Tüter is an academic researcher from Istanbul Technical University. The author has contributed to research in topics: Lipase & Triacylglycerol lipase. The author has an hindex of 14, co-authored 29 publications receiving 701 citations.

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Immobilized Candida antarctica lipase-catalyzed alcoholysis of cotton seed oil in a solvent-free medium.

TL;DR: The results indicated that alcoholysis products of cotton seed oil could be used as valuable intermediates in oleochemistry.
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Transesterification reaction of the fat originated from solid waste of the leather industry

TL;DR: The effect of oil/alcohol molar ratio, the amount of catalyst and temperature on ester production was individually investigated and optimum reaction conditions were determined, and the fuel properties of the ester product were studied according to the EN 14214 standard.
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Esterification Reaction of Oleic Acid With a Fusel Oil Fraction for Production of Lubricating Oil

TL;DR: In this paper, the esterification of oleic acid with a fraction of fusel oil was investigated and the variables that affect ester yield, such as temperature, molar ratio of OE to alcohol, and amount of catalyst, were determined Powdered silica gel was chosen to remove water instead of granular silica, magnesium sulfate, or benzene.
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Development of the julia asymmetric epoxidation reaction. part 2. application of the oxidation to alkyl enones, enediones and unsaturated keto esters

TL;DR: In this article, a polyleucine-based system has been used to catalyse the asymmetric oxidation of a variety of alkyl enones 1−4, 9−14, an enynone 16 and a dienone 17 to afford the corresponding epoxides 5−8, 18−26 in good to excellent yield and optical purity.
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Solvent-free glycerolysis of palm and palm kernel oils catalyzed by commercial 1,3-specific lipase from Humicola lanuginosa and composition of glycerolysis products

TL;DR: Glycerolysis of palm and palm kernel oils were conducted using a commercial 1,3-specific lipase from Humicola lanuginosa (trade name: SP 398) as catalyst (500 units lipase g−1 oil) at 40 °C and oil:glycerol (1:2 mol mol−1) in a solvent-free system as discussed by the authors.