Study of some physico-chemical characteristics of a Saccharomyces cerevisiae endopolygalacturonase: a possible use in beverage industry

Belarbi, A.; Hachet, C; Helfer, A-C; Gognies, Sabine; Gainvors, A.

doi:10.1038/sj.jim.2900820

Cited by 8 publications

(7 citation statements)

References 15 publications

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“…The protein profile analyzed by SDS-PAGE showed the presence of multiple protein bands, around molecular weight 30 -50 KDa, which confirms the presence of pectinase enzyme. This result resembled with the previous work [13], (Figure 8). In zymogram the SDS-PAGE containing pectinase was detected by gel coat.…”

Section: Sds Page and Zymogramsupporting

confidence: 92%

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Production of Extracellular Pectinase by Bacillus Cereus Isolated From Market Solid Waste

Elangovan¹,

D²,

Mariappan³

et al. 2011

JBABM

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Introduction Enzymes are biocatalysts which are synthesized by living cells. chemical reaction. Many bacteria, fungi and higher plants are known to produce pectinolytic enzyme called pectinase, that breakdown pectin, a polysaccharide substrate that is found in the cell wall of plants. One of the most important and widely used commercial pectinase by Henri Braconnot (1825). Pectin is the jelly like matrix structural polysaccharide found in primary cell wall and middle lamella of fruits applications in the production of oligogalacturonides as functional food components [2]. Bacillus cereus is an endemic, soil dwelling, Gram-positive, rod-shaped, beta hemolytic bacterium. Bacillus sp was discovered by Cohn and Koch in the 19 th Bacillus cereus group is composed of B. anthracis, B. cereus, B. mycoides, B. pseudomycoides, B. thuringiensis and B. weihenstephanensis capacity of selected Bacillus sp to produce and secrete large quantities (20-25 g/L) of extracellular enzymes has placed them among the most important industrial enzyme producers [5]. Pectic substances are widely distributed in fruits and vegetables (10-30% in turnips peels of orange and in pulps of tomato, pineapple and lemon); hence they form important natural substrates for pectinases. Pectinases are mainly used Material and Methods Materials

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Section: Sds Page and Zymogramsupporting

confidence: 92%

“…The protein profile and the presence of enzyme were confirmed by SDS PAGE analysis [13]. The SDS-PAGE was performed in 13 % (w/v) gels and samples were heated for 10 min at 45°C in the sample buffer before loading on wells.…”

Section: Sds Page Analysis and Zymography Of Pectinasementioning

confidence: 99%

Production of Extracellular Pectinase by Bacillus Cereus Isolated From Market Solid Waste

Elangovan¹,

D²,

Mariappan³

et al. 2011

JBABM

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“…Alana et al (1989) also reported the optimum pH for PL production in the range of 6 to 7. According to Belarbi et al (2000), the pH optimum was in between 4.0 to 5.5 for PG and also reported an endo PG which was active at temperatures from 4 to 50 o C.…”

Section: Effect Of Temperature and Ph On Polygalacturonase (Pg) And Pmentioning

confidence: 96%

Low temperature active pectinases production by Saccharomyces cerevisiae isolate and their characterization

Poondla

Bandikari

Subramanyam

et al. 2015

Biocatalysis and Agricultural Biotechnology

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“…The PGU1‐1 gene encoding the endoPG of this strain has been cloned and overexpressed (Gognies et al ., 1999). The corresponding Pgu1 ‐ 1p protein has been purified and characterized (Belarbi et al ., 2000; Gainvors et al ., 2000). Unexpectedly, the protein sequence of Pgu1 ‐ 1p from SCPP presents only three different amino acids from the protein sequence of Pgu1 ‐ 2p, the endoPG of the negative control laboratory strain X2180 ‐ 1B (Gognies et al ., 1999).…”

Section: Introductionmentioning

confidence: 99%

Regulation of the expression of endopolygalacturonase gene PGU1 in Saccharomyces

Gognies¹,

Simon²,

Belarbi³

2001

Yeast

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Previous work in our laboratory has shown that Saccharomyces bayanus strain SCPP is the only reported yeast expressing the three types of pectolytic enzymes: pectin esterases, pectin lyases and polygalacturonases. One of these enzymes, the endopolygalacturonase (endoPG), hydrolyses plant-speci®c polysaccharide pectin. The endoPG encoding gene (PGU1) is also present in Saccharomyces cerevisiae. It has been shown that this endoPG is required for the development of pseudohyphae. Using genomic DNA, the PGU1-1 and PGU1-2 promoters of these strains have been ampli®ed and used to construct gene fusions with the b-galactosidase gene. On the basis of b-galactosidase measurements, we compared the expression of both promoters in different environmental conditions in order to identify their modulation. We have shown that the PGU1 gene is upregulated by the presence of the pectin and the product resulting from endopolygalacturonase activity. Moreover, expression of the PGU1 is also enhanced under respiratory and ®lament formation conditions.

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Study of some physico-chemical characteristics of a Saccharomyces cerevisiae endopolygalacturonase: a possible use in beverage industry

Cited by 8 publications

References 15 publications

Production of Extracellular Pectinase by Bacillus Cereus Isolated From Market Solid Waste

Production of Extracellular Pectinase by Bacillus Cereus Isolated From Market Solid Waste

Low temperature active pectinases production by Saccharomyces cerevisiae isolate and their characterization

Regulation of the expression of endopolygalacturonase gene PGU1 in Saccharomyces

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