Inhibition of Rhizomucor miehei and Candida rugosa lipases by d-glucose in esterification between l-alanine and d-glucose

Somashekar, Bhandya R.; Lohith, K.; Manohar, B.; Divakar, Soundar

doi:10.1263/jbb.103.122

Cited by 12 publications

(4 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…A competitive inhibition of the lipase activity by the acyl-group acceptor is well described for short-chained alcohols or D-glucose (Bousquet-Dubouch et al 2001;Somashekar et al 2007). However, to achieve higher conversion yields, a more extensive study is necessary, examining factors like the intervals in which MAG is added and the amounts which are added.…”

Section: Influence Of Reaction Time On Enzymatic De-acidificationmentioning

confidence: 93%

Enzymatic esterification of free fatty acids in vegetable oils utilizing different immobilized lipases

et al. 2014

View full text Add to dashboard Cite

Different immobilized lipases were screened for their ability to esterify free fatty acids (FFA) with monoacylglycerol (MAG) as acyl-group acceptor. A lipase from Rhizomucor miehei (Lipozyme RMIM) was the most suitable for lipase-catalyzed de-acidification-a promising alternative to conventional neutralization. A reduction of the FFA content to 0.6 % (w/w) was achieved by applying a substrate with an initial FFA-content of 6 % (w/w), the reaction at 50 °C for 22 h as well as the stepwise addition of a quadruple stoichiometric amount of MAG.

show abstract

Section: Influence Of Reaction Time On Enzymatic De-acidificationmentioning

confidence: 93%

Enzymatic esterification of free fatty acids in vegetable oils utilizing different immobilized lipases

et al. 2014

View full text Add to dashboard Cite

show abstract

“…-Glucose has been shown to be a competitive inhibitor in CRL-catalysed esterifications forming a dead-end complex. [38] Probably also 1a and 1d could bind to the active site of the enzyme in a non-productive manner blocking further catalysis. Also, larger molecules as saponins, flavonoids, alkaloids and antimicrobial agents are known inhibitors of CRL without their detailed mechanism of action been clear.…”

Section: Conversion (%)mentioning

confidence: 99%

Regioselective C‐6 Hydrolysis of MethylO‐Benzoyl‐pyranosides Catalysed byCandida RugosaLipase

Esmurziev

Sundby²,

Hoff

2009

Eur J Org Chem

View full text Add to dashboard Cite

Hydrolysis of six methyl O‐benzoyl‐pyranosides has been investigated using Candida rugosa lipase in dioxane/buffer mixtures. The lipase catalysed the hydrolysis of all substrates in a regiospecific manner at C‐6. The rate of reaction was dependent on pyranoside structure, reaction temperature and scale, dioxane concentration and agitation speed. Starting from their C‐6 O‐benzoyl precursors, the methyl 2,3,4‐tri‐O‐benzoyl‐pyranosides of α‐D‐galactose, β‐D‐galactose, α‐D‐glucose, and methyl 2,3‐di‐O‐benzoyl‐α‐D‐galactopyranoside could be isolated in 85–96 % yield. In hydrolysis of methyl 2,3,4,6‐tetra‐O‐benzoyl‐α‐D‐glucopyranoside and methyl 2,3,4,6‐tetra‐O‐benzoyl‐β‐D‐galactopyranoside substrate inhibition were observed, which in part could be overcome by increasing the reaction volume. Methyl 2,3,4,6‐tetra‐O‐benzoyl‐β‐D‐glucopyranoside and methyl 2,3,4,6‐tetra‐O‐benzoyl‐α‐D‐mannopyranoside were poor substrates for Candida rugosa lipase and low degree of conversion towards products were obtained under all conditions. No acyl migration was detected in any of the products.(© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009)

show abstract

“…A wide range of flavors has been obtained with the use of this catalyst, including farnesyl laurate (Rahman et al, 2010), butyl butyrate (Lorenzoni et al, 2012) and hexyl laurate (Chang et al, 2007). Furthermore, its suitability for ester synthesis has been evaluated under different conditions of temperature and pressure (Noel and Combes, 2003), water content (Valivety et al, 1992) and substrates (Somashekar et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Stability of immobilized Rhizomucor miehei lipase for the synthesis of pentyl octanoate in a continuous packed bed bioreactor

Skoronski

Padoin

Soares

et al. 2014

Braz. J. Chem. Eng.

View full text Add to dashboard Cite

-The enzymatic synthesis of organic compounds in continuous bioreactors is an efficient way to obtain industrially important chemicals. However, few works have focused on the study of the operational conditions and the bioprocess performance. In this work, the aliphatic ester pentyl octanoate was obtained by direct esterification using a continuous packed bed bioreactor containing the immobilized enzyme Lipozyme ® RM IM as catalyst. Enzymatic deactivation was evaluated under different conditions for the operational parameters substrate/enzyme ratio (5.00, 1.67, 0.83 and 0.55 mmol substrate ·min -1 ·g -1 enzyme ) and temperature (30, 40, 50 and 60 °C). The optimal condition was observed at 30 ºC, which gave the minimum enzymatic deactivation rate and the maximum conversion to the desired product, yielding approximately 60 mmols of ester for an enzyme loading of 0.5 g into the bioreactor. A first-order deactivation model showed good agreement with the experimental data.

show abstract

Inhibition of Rhizomucor miehei and Candida rugosa lipases by d-glucose in esterification between l-alanine and d-glucose

Cited by 12 publications

References 20 publications

Enzymatic esterification of free fatty acids in vegetable oils utilizing different immobilized lipases

Enzymatic esterification of free fatty acids in vegetable oils utilizing different immobilized lipases

Regioselective C‐6 Hydrolysis of MethylO‐Benzoyl‐pyranosides Catalysed byCandida RugosaLipase

Stability of immobilized Rhizomucor miehei lipase for the synthesis of pentyl octanoate in a continuous packed bed bioreactor

Contact Info

Product

Resources

About