A new lipase (Alip2) with high potential for enzymatic hydrolysis of the diester diethyladipate to the monoester monoethyladipate

Nietz, Daniela; Bode, R.; Kunze, Gotthard; Rauter, Marion

doi:10.1016/j.enzmictec.2021.109898

Cited by 5 publications

(8 citation statements)

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“…Compared to the chemical synthesis, lower temperatures and alcohol concentrations have to be used. Some lipases and pig liver esterase have already been successfully used for the monohydrolysis of various diesters [24][25][26][27][28][29][30]. Under the conditions tested, high monoester yields of 96 to 99+% were obtained [24,26,27].…”

Section: Structurementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Some lipases and pig liver esterase have already been successfully used for the monohydrolysis of various diesters [ 24 , 25 , 26 , 27 , 28 , 29 , 30 ]. Under the conditions tested, high monoester yields of 96 to 99+% were obtained [ 24 , 26 , 27 ]. It is no foregone conclusion that lipases/esterases carry out chemoselective hydrolysis of only one of the two ester functions of the diester compound.…”

Section: Introductionmentioning

confidence: 99%

“…Nietz et al describe the aliphatic diester hydrolysis of diethyl adipate (DEA) by purified intracellular lipase Alip2-c6hp expressed in Blastobotrys raffinosifermentans . This reaction produced 96% monoethyl adipate (MEA), and only 1.6% of the unwanted side-product adipic acid (AA) [ 27 ]. Other aliphatic dicarboxylic acid esters were completely hydrolyzed to their corresponding monoesters [ 27 ].…”

Section: Introductionmentioning

confidence: 99%

“…This reaction produced 96% monoethyl adipate (MEA), and only 1.6% of the unwanted side-product adipic acid (AA) [ 27 ]. Other aliphatic dicarboxylic acid esters were completely hydrolyzed to their corresponding monoesters [ 27 ]. Aliphatic monoester as MEA and derivatives thereof have positive effects on pathogen attacked plants by activating resistance mechanisms, thus improving protective effects [ 34 , 35 , 36 , 37 ].…”

Section: Introductionmentioning

confidence: 99%

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Cutinase ACut2 from Blastobotrysraffinosifermentans for the Selective Desymmetrization of the Symmetric Diester Diethyl Adipate to the Monoester Monoethyl Adipate

Rauter¹,

Nietz

Kunze

2022

Microorganisms

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Monoethyl adipate (MEA) is a highly valuable monoester for activating resistance mechanisms and improving protective effects in pathogen-attacked plants. The cutinase ACut2 from the non-conventional yeast Blastobotrys (Arxula) raffinosifermentans (adeninivorans) was used for its synthesis by the desymmetrization of dicarboxylic acid diester diethyl adipate (DEA). Up to 78% MEA with 19% diacid adipic acid (AA) as by-product could be synthesized by the unpurified ACut2 culture supernatant from the B. raffinosifermentans overexpression strain. By adjusting pH and enzyme concentration, the selectivity of the free ACut2 culture supernatant was increased, yielding 95% MEA with 5% AA. Selectivity of the carrier immobilized ACut2 culture supernatant was also improved by pH adjustment during immobilization, as well as carrier enzyme loading, ultimately yielding 93% MEA with an even lower AA concentration of 3–4%. Thus, optimizations enabled the selective hydrolysis of DEA into MEA with only a minor AA impurity. In the up-scaling, a maximum of 98% chemical and 87.8% isolated MEA yield were obtained by the adsorbed enzyme preparation with a space time yield of 2.6 g L−1 h−1. The high monoester yields establish the ACut2-catalyzed biosynthesis as an alternative to existing methods.

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