Esterases of lactic acid bacteria and cheese flavour: Milk fat hydrolysis, alcoholysis and esterification

Holland, Ross; Liu, S.-Q.; Crow, Vaughan L.; Delabre, Marie-Laure; Lubbers, Mark W.; Bennett, Michael J.; Norris, G.

doi:10.1016/j.idairyj.2004.09.012

Cited by 158 publications

(110 citation statements)

References 39 publications

(80 reference statements)

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“…Other reports from our group on the esterase activity (41) and ␤-glucosidase activity (26)(27)(28) of LAB isolates describe a similar enhancement of activity by ethanol when assaying whole cells. While the need for ethanol to enhance ester formation in cheese has been reported, only levels of 6% (vol/vol) have been assessed (33). There are no reports in the literature of LAB esterases retaining activity at 50% ethanol, although an esterase from Bacillus (54).…”

Section: Discussionmentioning

confidence: 99%

Cloning and Characterization of an Intracellular Esterase from the Wine-Associated Lactic Acid BacteriumOenococcus oeni

Sumby

Matthews

Grbin

et al. 2009

Appl Environ Microbiol

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We report the cloning and characterization of EstB28, the first esterase to be so characterized from the wine-associated lactic acid bacterium, Oenococcus oeni. The published sequence for O. oeni strain PSU-1 was used to identify putative esterase genes and design PCR primers in order to amplify the corresponding region from strain Ooeni28, an isolate intended for inoculation of wines. In this way a 912-bp open reading frame (ORF) encoding a putative esterase of 34.5 kDa was obtained. The amino acid sequence indicated that EstB28 is a member of family IV of lipolytic enzymes and contains the GDSAG motif common to other lactic acid bacteria. This ORF was cloned into Escherichia coli using an appropriate expression system, and the recombinant esterase was purified. Characterization of EstB28 revealed that the optimum temperature, pH, and ethanol concentration were 40°C, pH 5.0, and 28% (vol/vol), respectively. EstB28 also retained marked activity under conditions relevant to winemaking (10 to 20°C, pH 3.5, 14% [vol/vol] ethanol). Kinetic constants were determined for EstB28 with p-nitrophenyl (pNP)-linked substrates ranging in chain length from C 2 to C 18 . EstB28 exhibited greatest specificity for C 2 to C 4 pNP-linked substrates.

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Section: Discussionmentioning

confidence: 99%

Cloning and Characterization of an Intracellular Esterase from the Wine-Associated Lactic Acid BacteriumOenococcus oeni

Sumby

Matthews

Grbin

et al. 2009

Appl Environ Microbiol

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“…Esta evolução pode ser relacionada à proliferação das bactérias psicrotróficas lipolíticas e das bactérias lácticas, as quais produzem enzimas lipolíticas responsáveis em hidrolisar lipídios liberando ácidos graxos livres entre outros compostos voláteis (HOLLAND, et al 2005 …”

Section: Análises Físico-químicas E Químicasunclassified

Estudo da vida útil de queijo Minas

Sangaletti¹,

Porto²,

Brazaca³

et al. 2009

Ciênc. Tecnol. Aliment.

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“…An opposite result about LAB was reported by Liu et al [23] who found that decreasing water activity (from 0.99 to 0.80) considerably reduced the intracellular esterase I activity from S. thermophiles. Holland et al [3] reported that esterase of LAB released short-chain FFA from milk fat at high water activity and synthesized short-chain ethyl esters at low water activity during ripening.…”

Section: Influence Of Aw On Esterase Activitymentioning

confidence: 99%

“…[2] These are common volatile components of flavour in fermented products, providing the desirable fruity aroma to the overall profile of wines and dairy products. [3,4] Esterase and lipase are the main enzymes that are responsible for the formation of these compounds. [5] More information is found about the enzymatic synthesis by microbial esterase in fermented products, such as yeast in wine and lactic acid bacteria (LAB) in cheese.…”

Section: Introductionmentioning

confidence: 99%

Esterase activities of autochthonous starter cultures to increase volatile flavour compounds in Chinese traditional fermented fish (Suan yu)

Gao

Jiang

et al. 2017

International Journal of Food Properties

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Suan yu, a type of Chinese traditional fermented freshwater fish in solid form, is cheered among consumers due to its characteristic sensory flavour, primarily taste and smell. The purpose of this study was to investigate the presence of esterase activity of Lactobacillus plantarum 120, Staphylococcus xylosus 135, and Saccharomyces cerevisiae 31, in selecting appropriate processing means to accelerate the formation of the desired flavour in Suan yu. The results showed that all strains exhibited esterase activities in both intracellular and extracellular fractions against p-nitrophenyl (p-NP)-acetate, p-NP-butyrate, and p-NP-octanoate, and also that the maximum activity was observed in the intracellular fraction with p-NP-octanoate. Esterase activities of all strains were inhibited by low pH and low water activity (Aw), with the exception of L. plantarum 120 exhibiting an increase in intracellular activity with decreasing Aw. Moreover, L. plantarum 120 and S. xylosus 135 esterase were negatively affected by decreasing temperature, while a positive influence was observed on the intracellular esterase of S. cerevisiae 31. The results suggested that a low pH, a low Aw and a high temperature would be more appropriate for Suan yu processing to produce more flavour compounds which are acceptable by consumers. ARTICLE HISTORY

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Esterases of lactic acid bacteria and cheese flavour: Milk fat hydrolysis, alcoholysis and esterification

Cited by 158 publications

References 39 publications

Cloning and Characterization of an Intracellular Esterase from the Wine-Associated Lactic Acid BacteriumOenococcus oeni

Cloning and Characterization of an Intracellular Esterase from the Wine-Associated Lactic Acid BacteriumOenococcus oeni

Estudo da vida útil de queijo Minas

Esterase activities of autochthonous starter cultures to increase volatile flavour compounds in Chinese traditional fermented fish (Suan yu)

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