Cloning, Expression, Purification, and Characterization of a Novel Esterase from Lactobacillus plantarum

Brod, Fábio Cristiano Angonesi; Vernal, Javier; Bertoldo, Jean B.; Terenzi, Hernán; Arisi, Ana Carolina Maisonnave

doi:10.1007/s12033-009-9232-2

Cited by 39 publications

(36 citation statements)

References 25 publications

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“…Numerous reports have been published on the cloning and expression of microbial esterases (Brod et al 2010;Huang et al 2010;Terahara et al 2010;Ro et al 2004;Khalameyzer et al 1999). When considering heterologous expression, one needs to investigate the type of expression system to be applied, as this could have a significant effect on the level of enzymes produced.…”

Section: Heterologous Production Of Esterasesmentioning

confidence: 99%

Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

2017

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Abstract:In the pulp and paper industry, during the manufacturing process, the agglomeration of pitch particles (composed of triglycerides, fatty acids, and esters) leads to the formation of black pitch deposits in the pulp and on machinery, which impacts on the process and pulp quality. Traditional methods of pitch prevention and treatment are no longer feasible due to environmental impact and cost. Consequently, there is a need for more efficient and environmentally friendly approaches. The application of lipolytic enzymes, such as lipases and esterases, could be the sustainable solution to this problem. Therefore, an understanding of their structure, mechanism, and sources are essential. In this report, we review the microbial sources for the different groups of lipolytic enzymes, the differences between lipases and esterases, and their potential applications in the pulping industry.

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Section: Heterologous Production Of Esterasesmentioning

confidence: 99%

Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

2017

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“…Esterases that originate from wine LAB are responsible for both the biosynthesis and hydrolysis of esters (Matthews et al, 2004;Sumby et al, 2009;Brod et al, 2010). Oenococcus oeni, as well as species of Lactobacillus and Pediococcus, is able to hydrolyse esters and Matthews et al (2006) found that significant esterase activity levels remained under wine-like conditions.…”

Section: Malolactic Fermentation Must and Wine Composition Before Inomentioning

confidence: 99%

“…There is great variation between species and genera with regards to their esterase activity and from available literature, it seems as if O. oeni displays the greatest activity, compared to lactobacilli and pediococci (Matthews et al, 2006). Recently, Brod et al (2010) characterised a novel esterase from L. plantarum and found substrate specificity towards p-nitrophenyl-linked substrates, similar to that of O. oeni (Matthews et al, 2006).…”

Section: Malolactic Fermentation Must and Wine Composition Before Inomentioning

confidence: 99%

“…Some of the aroma-related enzymes include β-glucosidase, phenolic acid decarboxylase (PAD), citrate lyase, esterase, protease, peptidases, α-acetolactate synthase and α-acetolactate reductase (Spano et al, 2005;Sumby et al, 2009;Brod et al, 2010;Mtshali et al, 2010), as well as enzymes that play a role in the production of volatile sulphur compounds, including S-adenosylmethionine synthase, cystathionine β/γ-lyase and glutathione reductase (Knoll et al, 2010). Other enzymes of interest that play a negative role in the wholesomeness of the wine, besides those enzymes implicated in biogenic amine production, include those that are involved in ethyl carbamate formation, a potential carcinogen.…”

Section: Introductionmentioning

confidence: 99%

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Selection and Characterisation of Oenococcus oeni and Lactobacillus plantarum South African Wine Isolates for Use as Malolactic Fermentation Starter Cultures

Lerm¹,

Engelbrecht²,

Toit³

2016

SAJEV

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This study focused on characterising 23 Oenococcus oeni and 19 Lactobacillus plantarum strains isolated from the South African wine environment for the development of potential commercial malolactic fermentation (MLF) starter cultures. These strains were characterised with regards to oenological important characteristics, including the genetic screening for enzyme-encoding genes (enzymes that are involved/implicated in wine aroma modification, as well as enzymes pertaining to the wholesomeness of the final wine product), their fermentation capabilities, the ability to maintain viability during MLF, as well as the volatile acidity production. A total of three O. oeni and three L. plantarum strains were selected at the completion of this study. These six strains showed the most potential during the characterisation stages of the study and were able to successfully complete MLF in Pinotage wine. It was also found that L. plantarum strains displayed a more diverse enzyme profile than O. oeni strains, particularly with regards to the presence of the aroma-modifying enzymes β-glucosidase and phenolic acid decarboxylase (PAD), which implies the future use of this species in the modification of the wine aroma profile and use as commercial starter culture.

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“…Lactobacillus plantarum is a lactic acid bacterial species that is most abundant in fermenting plant-derived raw materials and also might colonize the human gastrointestinal tract considerably better than other tested lactobacilli (10). Although several esterase enzymes have been described in L. plantarum (11)(12)(13)(14)(15)(16)(17)(18)(19)(20), cinnamoyl esterase activity has not been found yet.Feruloyl esterases constitute an interesting group of enzymes with a potentially broad range of applications in the food industry, and there is a constant search for such enzymes with more desirable properties for novel food applications; the present study represents the description of a feruloyl esterase enzyme in L. plantarum that is widely distributed among strains of the species. …”

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confidence: 99%

Characterization of a Feruloyl Esterase from Lactobacillus plantarum

Esteban-Torres

Reverón

Mancheño

et al. 2013

Appl Environ Microbiol

119

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bLactobacillus plantarum is frequently found in the fermentation of plant-derived food products, where hydroxycinnamoyl esters are abundant. L. plantarum WCFS1 cultures were unable to hydrolyze hydroxycinnamoyl esters; however, cell extracts from the strain partially hydrolyze methyl ferulate and methyl p-coumarate. In order to discover whether the protein Lp_0796 is the enzyme responsible for this hydrolytic activity, it was recombinantly overproduced and enzymatically characterized. Lp_0796 is an esterase that, among other substrates, is able to efficiently hydrolyze the four model substrates for feruloyl esterases (methyl ferulate, methyl caffeate, methyl p-coumarate, and methyl sinapinate). A screening test for the detection of the gene encoding feruloyl esterase Lp_0796 revealed that it is generally present among L. plantarum strains. The present study constitutes the description of feruloyl esterase activity in L. plantarum and provides new insights into the metabolism of hydroxycinnamic compounds in this bacterial species. Phenolic acids are abundant, naturally occurring molecules that contribute to the rigidity of plant cell walls. Hydroxycinnamic acids, such as ferulic, sinapic, caffeic, and p-coumaric acids, are found both covalently attached to the cell wall and as soluble forms in the cytoplasm. Esters and amides are the most frequently reported types of conjugates, whereas glycosides occur only rarely (1). Hydroxycinnamates are found in numerous plant foods and in significant quantities in agroindustry-derived by-products. The industrial use of hydroxycinnamates has attracted growing interest since they and their conjugates were shown to be bioactive molecules possessing potential antioxidant activities and health benefits. The removal of these phenolic compounds and the breakdown of the ester linkages between polymers allow their exploitation for numerous industrial and food applications.Feruloyl esterases, also known as ferulic acid esterases, cinnamic acid esterases, or cinnamoyl esterases, are the enzymes involved in the release of phenolic compounds, such as ferulic, pcoumaric, caffeic, and sinapic acids, from plant cell walls (2). In human and ruminal digestion, feruloyl esterases are important to de-esterify dietary fiber, releasing hydroxycinnamates and derivatives, which have been shown to have positive effects, such as antioxidant, anti-inflammatory, and antimicrobial activities (3). They are also involved in colonic fermentation, where their activities in the microbiota improve the breakdown of ester bonds in hydroxycinnamates (3). The biological properties of hydroxycinnamates depend on their absorption and metabolism. Although there is evidence that food hydroxycinnamates are degraded by the gut microbiota, only limited information on the microorganisms and enzymes involved in this degradation is currently available.Feruloyl esterases able to hydrolyze hydroxycinnamates have been found in lactic acid bacteria isolated from foods and from the human intestinal microbiota, such as some str...

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Cloning, Expression, Purification, and Characterization of a Novel Esterase from Lactobacillus plantarum

Cited by 39 publications

References 25 publications

Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

Selection and Characterisation of Oenococcus oeni and Lactobacillus plantarum South African Wine Isolates for Use as Malolactic Fermentation Starter Cultures

Characterization of a Feruloyl Esterase from Lactobacillus plantarum

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