Enzymatic reactions and synthesis of n-butyl caproate: esterification, transesterification and aminolysis using a recombinant lipase from Geobacillus thermoleovorans CCR11.
The recombinant lipase LipMatCCR11 from the thermophilic strain Geobacillus thermoleovorans CCR11 was applied in the synthesis of n-butyl caproate via transesterification in hexane and xylene. The short chain flavour ester was obtained by alcoholysis from ethyl caproate and n-butyl alcohol and acidolysis from n-butyl butyrate and caproic acid. This enzyme was also used in the condensation reaction from caproic acid and n-butanol. The conversion percentages at equilibrium (Xe) were similar to those obtained with Candida antarctica lipase fraction B (CAL-B) in the same reaction conditions, while lower conversion velocities (k) were attained. LipMatCCR11 reached high conversion percentages in either hexane or xylene as organic media (> 63%); the enzyme was also able to catalyze the aminolysis reaction of ethyl caproate with benzyl amine in hexane obtaining a conversion percentage > 62%.
Sánchez-Otero
M Guadalupe
MG
Instituto Tecnológico de Veracruz, Unidad de Investigación y Desarrollo en Alimentos, Av. Miguel A. de Quevedo 2779, Veracruz 91897, México.
Quintana-Castro
Rodolfo
R
Mora-González
Paola C
PC
Márquez-Molina
Ofelia
O
Valerio-Alfaro
Gerardo
G
Oliart-Ros
Rosamaría
R
D000475:Alkenes / Q000737:chemistry; D002208:Caproates / Q000737:chemistry / Q000378:metabolism*; D004951:Esterification; D056506:Geobacillus / Q000201:enzymology* / Q000235:genetics; D007700:Kinetics; D008049:Lipase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014992:Xylenes / Q000737:chemistry
D000475:Alkenes; D002208:Caproates; D011994:Recombinant Proteins; D014992:Xylenes; C117224:1-hexene; C046398:butyl caprylate; D008049:Lipase