Hidroliza triacetina z  uporabo encima lipaze : diplomsko delo visokošolskega strokovnega študijskega programa I. stopnje

Belina, Nina

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Title:	Hidroliza triacetina z uporabo encima lipaze : diplomsko delo visokošolskega strokovnega študijskega programa I. stopnje
Authors:	ID Belina, Nina (Author) ID Pečar, Darja (Mentor) More about this mentor... ID Goršek, Andreja (Comentor)
Files:	VS_Belina_Nina_2021.pdf (2,01 MB) MD5: 104E360E87BC4A3F3BCA37B2386AB707 PID: 20.500.12556/dkum/3a94351a-e9a5-48b6-8017-076311274243
Language:	Slovenian
Work type:	Bachelor thesis/paper
Typology:	2.11 - Undergraduate Thesis
Organization:	FKKT - Faculty of Chemistry and Chemical Engineering
Abstract:	V diplomskem delu smo preučevali reakcijo hidrolize triacetina pri različnih pogojih. Reakcije smo najprej izvajali v fosfatnem pufru (c = 0,05 mol/L), pri pH = 7, kateremu smo dodali 1 mL 99 % triacetina. Reakcije so potekale pri (25, 30 in 35) °C in z različnimi količinami dodanega katalizatorja – encima lipaze (0,2; 0,4 in 0,6) g. Za primerjavo smo izvedli reakcije z 0,5 in 2 mL triacetina pri vseh treh temperaturah in 0,2 g lipaze. Na koncu smo se odločili izvesti dve reakciji pri najvišji temperaturi in največji količini dodane lipaze z 1 mL triacetina in fosfatnim pufrom s pH=6 in 8. Za spremljanje reakcij smo uporabili in- situ ReactIR 702L, podjetja Mettler Toledo. Ugotovili smo, da dosežemo pri reakciji izvedeni pri 35 °C, z 0,6 g dodane lipaze in pri pH=7 in 8 najvišjo presnovo. Iz rezultatov je razvidno, da je reakcijska hitrost višja pri višjem pH. Dobljene rezultate smo opisali z Michaelis-Menten-inim modelom. Povprečne Michaelis-Menten-ine konstante so 103,9; 104,8 in 238,3 mol/L in aktivacijske energije 104,2; 109,3 in 64,3 kJ/mol za reakcije z 0,2; 0,4 in 0,6 g dodane lipaze. Izračunane konstante proizvodnosti so manjše pri nižji temperaturi in manjši količini dodane lipaze.
Keywords:	triacetin, hidroliza, diacetin, lipaza, FTIR
Place of publishing:	Maribor
Place of performance:	Maribor
Publisher:	[N. Belina]
Year of publishing:	2021
Number of pages:	X, 44 str.
PID:	20.500.12556/DKUM-79555
UDC:	66.094.941(043.2)
COBISS.SI-ID:	75916803
Publication date in DKUM:	08.09.2021
Views:	1365
Downloads:	157
Metadata:
Categories:	KTFMB - FKKT
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License:	CC BY-ND 4.0, Creative Commons Attribution-NoDerivatives 4.0 International

Link:	http://creativecommons.org/licenses/by-nd/4.0/
Description:	Under the NoDerivatives Creative Commons license one can take a work released under this license and re-distribute it, but it cannot be shared with others in adapted form, and credit must be provided to the author.
Licensing start date:	23.07.2021

Secondary language

Language:	English
Title:	Hydrolysis of triacetin using lipase enzyme
Abstract:	In the bachelor’s thesis, we studied the hydrolysis reaction of triacetin under different conditions. The reaction was carried out by the usage of phosphate buffer (c = 0,05 mol/L) at pH = 7, to which we added 1 mL of 99 % triacetin. Reactions took place at 25, 30 and 35 °C and with varying quantities of added catalyst – lipase enzyme (0,2; 0,4 and 0,6 g). For comparison, we carried out reactions with 0,5 and 2 mL of triacetin at all three temperatures and 0,2 g of lipase. In the end, we decided to perform two reactions at the highest temperature and the largest addition of lipase with 1 ml of triacetin and phosphate buffer at pH = 6 and pH = 8. For reaction observation, we used in situ ReactIR 702L from Mettler Toledo. We found out that the reactions at 35 °C with 0,6 g of lipase and pH = 7 and 8 had the most substantial conversion. The results also show that the reaction rates increase by the usage of pH = 8 buffer rather than the lower pH buffer. The obtained results were described with the Michaelis-Menten model. Average Michaelis-Menten constants were 103,9; 104,8 and 238,3 mol/L, and activation energies 104,2; 109,3 and 64,3 kJ/mol for 0,2; 0,4 and 0,6 g of added lipase. Obtained reaction rate constants were lower at lower temperatures and lower amounts of added lipase.
Keywords:	triacetin, diacetin, hydrolysis, lipase, FTIR

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