A novel esterase fromSaccharomyces carlsbergensis, a possible function for the yeastTIP1 gene

Horsted, Mette Wenzel; Dey, Estera Szwajcer; Holmberg, Steen; Kielland‐Brandt, Morten C.

doi:10.1002/(sici)1097-0061(19980630)14:9<793::aid-yea277>3.0.co;2-e

Cited by 18 publications

(2 citation statements)

References 30 publications

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“…The mutant lacking gene TIP1 (Δ TIP1 ) showed a reduced, albeit not significant, esterase activity compared to WT. Possibly, Tip1p has low affinity for cFDA as it has been described to hydrolyse fatty acid ethyl esters with a carbon size ranging from 4 to 16 [4], limiting Tip1p contribution towards acetate ester hydrolysis. It may also be possible that other esterases encoded on the genome partially compensate the loss of TIP1 .…”

Section: Discussionmentioning

confidence: 99%

“…Mutants lacking Iah1p showed an increase in isoamyl acetate, ethyl acetate and isobutyl acetate, which may suggest a reduction of hydrolysis of several acetate esters. TIP1 encodes for a protein with putative esterase activity towards esters of fatty acid chains ranging from 4 to 16 carbon atoms [4]. Therefore a knock-out of this gene may result in an increase of esters derived from free fatty acids and ethanol, like ethyl hexanoate and ethyl octanoate.…”

Section: Introductionmentioning

confidence: 99%

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CRISPR-Cas genome engineering of esterase activity in Saccharomyces cerevisiae steers aroma formation

2018

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ObjectiveSaccharomyces cerevisiae is used worldwide for the production of ale-type beers. This yeast is responsible for the production of the characteristic fruity aroma compounds. Esters constitute an important group of aroma active secondary metabolites produced by S. cerevisiae. Previous work suggests that esterase activity, which results in ester degradation, may be the key factor determining the abundance of fruity aroma compounds. Here, we test this hypothesis by deletion of two S. cerevisiae esterases, IAH1 and TIP1, using CRISPR-Cas9 genome editing and by studying the effect of these deletions on esterase activity and extracellular ester pools.ResultsSaccharomyces cerevisiae mutants were constructed lacking esterase IAH1 and/or TIP1 using CRISPR-Cas9 genome editing. Esterase activity using 5-(6)-carboxyfluorescein diacetate (cFDA) as substrate was found to be significantly lower for ΔIAH1 and ΔIAH1ΔTIP1 mutants compared to wild type (WT) activity (P < 0.05 and P < 0.001, respectively). As expected, we observed an increase in relative abundance of acetate and ethyl esters and an increase in ethyl esters in ΔIAH1 and ΔTIP1, respectively. Interestingly, the double gene disruption mutant ΔIAH1ΔTIP1 showed an aroma profile comparable to WT levels, suggesting the existence and activation of a complex regulatory mechanism to compensate multiple genomic alterations in aroma metabolism.Electronic supplementary materialThe online version of this article (10.1186/s13104-018-3788-5) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

CRISPR-Cas genome engineering of esterase activity in Saccharomyces cerevisiae steers aroma formation

2018

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Disruption and basic functional analysis of six novel ORFs of chromosome XV fromSaccharomyces cerevisiae

Lafuente

Gancedo

1999

Yeast

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We report the disruption and functional analysis of six open reading frames (ORFs) from chromosome XV, namely YOL155c, YOL154w, YOL119c, YOL118c, YOR301w and YOR306c, in FY1679 and CEN.PK2 backgrounds. We constructed replacement cassettes and cloned each ORF into the pRS416 centromeric plasmid. No obvious phenotype was observed for the corresponding deleted strains with respect to growth, mating or sporulation. YOL155c encodes a protein with a secretion signal and putative GPI‐anchor recognition site and is possibly a cell wall protein, although its deletion did not present morphogenetic defects under any of the conditions tested. Although YOL119c and YOR306c are members of the monocarboxylate permease family, the growth of the double disruptant in acetate, lactate and pyruvate was similar to that of the parental strains. Copyright © 1999 John Wiley & Sons, Ltd.

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A novel reactive perstraction system based on liquid‐core microcapsules applied to lipase‐catalyzed biotransformations

Wyss¹,

Stockar²,

Marison³

2005

Biotech & Bioengineering

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A novel reactive perstraction system has been developed based on liquid-core capsules, involving an enzyme-catalyzed reaction coupled with simultaneous in situ product recovery. Lipase-catalyzed reactions, hydrolysis of triprionin and nitrophenyl laurate, were selected to test the system and demonstrate the feasibility of immobilization of enzymes to the membranes of liquid-core capsules and the ability to extract hydrophobic products of the reaction within the capsule core. The lipase from Candida rugosa was immobilized to the microcapsules by adsorption and by covalent binding through activation with glutaraldehyde. In both cases improved temperature and operational stability were achieved. Both types of immobilization resulted in a basic shift of the pH optimum for activity, from 7.5 to 9.0. The presence of an organic phase within the capsule core allowed direct product separation and lead to a decrease in product inhibition of the lipase-catalyzed reaction.

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A novel esterase fromSaccharomyces carlsbergensis, a possible function for the yeastTIP1 gene

Cited by 18 publications

References 30 publications

CRISPR-Cas genome engineering of esterase activity in Saccharomyces cerevisiae steers aroma formation

CRISPR-Cas genome engineering of esterase activity in Saccharomyces cerevisiae steers aroma formation

Disruption and basic functional analysis of six novel ORFs of chromosome XV fromSaccharomyces cerevisiae

A novel reactive perstraction system based on liquid‐core microcapsules applied to lipase‐catalyzed biotransformations

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