Purification and characterization of an intracellular esterase 
from <i>Propionibacterium freudenreichii</i> ssp. <i>freudenreichii</i> ITG 14

Kakariari, Evangellia; Georgalaki, Marina; Kalantzopoulos, George; Tsakalidou, Effie

doi:10.1051/lait:2000140

Cited by 19 publications

(15 citation statements)

References 22 publications

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“…The FFAs content depended thus mainly on the PAB strain activity and varied from 1 to 3 in the Emmental cheeses made from thermised milk. These results were in accordance with many researchers which demonstrated in vitro the variability of lipolytic activities among PAB strains [13,14,24,31]. The frequent interaction between PAB and LAB on propionic fermentation is now well known [25,33].…”

Section: Discussionsupporting

confidence: 90%

“…Propionic acid bacteria (PAB) are well known for their high lipolytic activity, 10 to 100 times more than lactic acid bacteria [15,26]. In vitro studies as well as experimental cheeses have shown the release of FFAs by PAB [14,24,31,37]. The location of lipase in PAB remains controversial: intracellular, parietal and extracellular, or extracellular [13,30].…”

Section: Introductionmentioning

confidence: 99%

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Contribution of propionic acid bacteria to lipolysis of Emmental cheese

Chamba

Perreard

2002

Lait

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-Compared to many cheeses, lipolysis of Emmental is generally low. It concerns about 1-2% of cheese fat and the amount of free fatty acids (FFAs) varies from 2 to 7 g . kg -1 of ripened cheese. In this work, we studied the extent of lipolysis due to propionic acid bacteria (PAB). The release of FFAs during the ripening of Emmental cheeses made from microfiltered milk, with or without propionic acid bacteria (PAB) was followed. The usual cooking step in the cheese process (up to 50 o C and 30 min) inactivated the lipoprotein lipase (EC 3.1.1.34) and the main factor in the lipolysis of Emmental cheese was shown to be the lipolytic activity of PAB. This activity was strain-dependent and not related to the production of propionic acid in cheese. The most abundant FFAs were palmitic acid, oleic acid, myristic acid and stearic acid as in milk fat and it was concluded that lipolytic activity of PAB is non-specific. Lastly, an interaction still not elucidated was evidenced between certain PAB strains and thermophilic lactobacilli strains regarding lipolysis extent in Emmental cheese.propionic acid bacteria / lipolysis / free fatty acid / Emmental cheese Résumé -Contribution des bactéries propioniques à la lipolyse de l'emmental. La lipolyse est comme la protéolyse et la glycolyse un phénomène majeur de l'affinage des fromages. Comparativement à de nombreux autres fromages, la lipolyse de l'emmental est généralement limitée. Elle porte sur environ 1 à 2% de la matière grasse du fromage et la teneur en acides gras libres (AGL) varie de 2 à 7 g . kg -1 dans le fromage affiné. Dans plusieurs expérimentations en fromagerie pilote, nous avons étudié l'intensité de la lipolyse générée par les bactéries propioniques. La libération des AGL au cours de l'affinage d'emmentals fabriqués à partir de lait microfiltré ensemencé ou non en bactéries propioniques, démontre que la cuisson habituelle du caillé en cuve (au moins 50 o C pendant 30 min) inactive la lipoprotéine lipase (EC 3.1.1.34) et que l'activité lipolytique des bactéries propioniques est majoritairement responsable de la lipolyse de l'emmental. Cette activité est souche dépendante et n'est pas corrélée avec l'intensité de la fermentation propionique. Des lactobacilles thermophiles homofermentaires interagissent avec les bactéries propioniques sur la lipolyse de l'emmental, par un

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Section: Discussionsupporting

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Contribution of propionic acid bacteria to lipolysis of Emmental cheese

Chamba

Perreard

2002

Lait

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“…Our results agree well with the results reported that Hg (II) inhibited the esterases of Arthrobacter viscosus NRRL B-1973 [35], Propionibacterium freudenreichii ssp. freudenreichii ITG 14 [36], Bacillus subtilis NRRL 365 [37] and Arthrobacter nicotianae 9458 [38]. It has been suggested that these ions (Hg (II), Cu (II) and Co (II)) caused a direct inhibition of the catalytic site of esterase.…”

Section: Time (Min)mentioning

confidence: 99%

Biochemical studies on native and cross-linked aggregates of Aspergillus awamori feruloyl esterase

Fazary

Ismadji

2009

International Journal of Biological Macromolecules

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“…Several esterases have been characterized in P. freudenreichii (9,10,15,21,24). Most of these studies concern the characterization of intracellular enzymes.…”

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Identification of a Secreted Lipolytic Esterase in Propionibacterium freudenreichii , a Ripening Process Bacterium Involved in Emmental Cheese Lipolysis

Dherbécourt

Falentin

Jardin

et al. 2010

Appl Environ Microbiol

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Lipolysis plays an important role in the formation of cheese flavor. In Emmental cheese, the main part of lipolysis has been associated with the presence of Propionibacterium freudenreichii, a species used as a ripening culture. Our aim was to identify the most probable lipolytic esterase(s) involved in cheese lipolysis by P. freudenreichii. Since cheese lipolysis mainly occurs during P. freudenreichii growth, we hypothesized that P. freudenreichii possesses secreted lipolytic esterase(s). For 12 putative esterase genes previously identified from the genome of P. freudenreichii CIRM1, the level of expression was quantified by real-time reverse transcriptase (RT)-PCR, and the subcellular localization of esterases was predicted in silico. The esterase activity in extracellular and intracellular extracts of P. freudenreichii was characterized by zymography, and the extracellular esterases were identified by mass spectrometry. Finally, the best candidate was overexpressed in the same strain. All of the 12 genes encoding putative esterases were expressed. Esterase PF#279 was predicted to be secreted in the medium, PF#774 to be surface exposed, and the 10 remaining putative esterases to be intracellular. Zymography revealed that esterase activities in culture supernatant differed from the ones detected in intracellular extracts. PF#279 was identified as the sole esterase present in culture supernatant. Transformed P. freudenreichii CIRM1 clones overexpressing PF#279 showed 5 to 8 times more lipolytic activity on milk fat than the wild-type strain. Combining in silico, biochemical, and genetic approaches, we showed that PF#279 is the sole secreted esterase in P. freudenreichii and is active on milk fat. Therefore, it is likely a key component in cheese lipolysis by P. freudenreichii.

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Purification and characterization of an intracellular esterase from Propionibacterium freudenreichii ssp. freudenreichii ITG 14

Cited by 19 publications

References 22 publications

Contribution of propionic acid bacteria to lipolysis of Emmental cheese

Contribution of propionic acid bacteria to lipolysis of Emmental cheese

Biochemical studies on native and cross-linked aggregates of Aspergillus awamori feruloyl esterase

Identification of a Secreted Lipolytic Esterase in Propionibacterium freudenreichii , a Ripening Process Bacterium Involved in Emmental Cheese Lipolysis

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