Pectin lyase overproduction by Penicillium griseoroseum mutants resistant to catabolite repression

Lima, Juliana Oliveira; Pereira, Jorge Fernando; Araújo, Elza Fernandes de; Queiroz, Marisa Vieira de

doi:10.1016/j.bjm.2016.12.009

Cited by 13 publications

(6 citation statements)

References 34 publications

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“…Several fungal pectin lyase genes (pelA, pelB) had been isolated and characterized from Aspergillus niger (Gysler et al, 1990;Kusters-van et al, 1991;Kusters-van et al, 1992), A. oryzae (Kitamoto et al, 2001). Recently, Lima et al, (2017) reported that expression of pectinolytic genes is regulated by catabolic repression. In presence of easily available metabolites, CreA-like protein binds at the promoters of gene (5-SYGGRG-3) to inhibit the gene transcription (Kiesenhofer, 2016).…”

Section: Pectinase Producing Organismsmentioning

confidence: 99%

Microbial Pectinases: A Review on Molecular and Biotechnological Perspectives

Samanta¹

2019

J microb biotech food sci

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Pectinases are upcoming enzymes in the biotechnological sector. This large group of enzymes involves in break down of pectic polysaccharides, the major component of middle lamella in plant cell wall. The pectin degrading enzymes are categorized according to their mode of action and release of degradative products. Various filamentous fungi, yeast, and bacteria are the common sources of microbial pectinases. Solid state fermentation is more preferable for extracellular microbial pectinases production over the submerged fermentation. A group of genes regulates the expression of pectinolytic enzymes. Mostly, all the enzymes share a common parallel  helix topology which consists of a single domain of parallel -strands folded into a large right-handed cylinder. These enzymes are eco-friendly tools for industrial applications and being used in various sectors like wine, food, paper industry, waste paper recycling, fruit juice preparation, processing of tea–coffee, animal feed preparation.

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Section: Pectinase Producing Organismsmentioning

confidence: 99%

Microbial Pectinases: A Review on Molecular and Biotechnological Perspectives

Samanta¹

2019

J microb biotech food sci

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“…Using submerged fermentation techniques, Antier et al 35 demonstrated that the dgrAW99-iii mutant produced 300% more pectinase than did the wild type strain Aspergillus niger C28B25. Lima et al 36 showed the enhanced pectin degradation abilities of Penicillium griseoroseum mutants (M02, M03, M04, M05, and M07) and selected sectors (M03 and M05) for pectin lyase (PL) production in liquid media due to their larger pectin degradation zones compared to those of the wild type.…”

Section: Discussionmentioning

confidence: 99%

Characterization of yeast mutant strains for starter culture in Arabica coffee fermentation

Meeampun,

Panyachanakul,

Samosorn

et al. 2024

Sci Rep

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Arabica coffee is the most popular and best-selling type of coffee. During coffee fermentation, microorganisms are essential for the production of metabolites and volatile compounds that affect coffee flavor quality. This work aimed to study the mutation, selection, and characterization of the Wickerhamomyces anomalus strain YWP1-3 as a starter culture to enhance the flavor quality of Arabica coffee. The results revealed that six mutants could produce relatively high levels of the pectinase enzyme on pectin agar media and exhibited high activity levels, ranging from 332.35 to 415.88 U/ml in mucilage broth. Strains UV22-2, UV22-3, UV41-1 and UV32-1 displayed higher levels of amylase activity than did the wild type. The UV22-2 and UV22-3 mutants exhibited the highest pectin degradation indices of 49.22% and 45.97%, respectively, and displayed significantly enhanced growth rates in nitrogen yeast base media supplemented with various sugars; thus, these mutants were evaluated for their ability to serve as a starter for fermentation of Arabica coffee. The cupping scores of coffees derived from UV22-2 and UV22-3 were 83.5 ± 1.5 and 82.0 ± 2.14, respectively. The volatile compounds in the roasted coffee fermented by UV22-2 were analyzed by GC‒MS, which revealed higher levels of furfuryl alcohol and furfuryl acetate than did the other samples. These findings suggested that UV22-2 could be an influential starter culture for Arabica coffee fermentation.

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“…Most pectin methylesterases (PGLs) degrade polygalacturonic acid and low-methoxyl pectin but exhibit less activity toward high-methoxyl pectin. In animals, the absence of endogenous pectinases hampers the digestion of pectin, making pectinase supplementation crucial for improving crude fiber utilization ( Sharma et al, 2012 ; Lima et al, 2017 ; Yang et al, 2020 ). Pectate lyase and pectin lyase act on the alpha-1,4-glycosidic bonds of pectin or pectinic acid, generating unsaturated pectin oligosaccharides without producing highly toxic methanol.…”

Section: Discussionmentioning

confidence: 99%

Feasibility insights into the application of Paenibacillus pabuli E1 in animal feed to eliminate non-starch polysaccharides

Li,

Yuan,

Jin

et al. 2023

Front. Microbiol.

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The goal of the research was to find alternative protein sources for animal farming that are efficient and cost-effective. The researchers focused on distillers dried grains with solubles (DDGS), a co-product of bioethanol production that is rich in protein but limited in its use as a feed ingredient due to its high non-starch polysaccharides (NSPs) content, particularly for monogastric animals. The analysis of the Paenibacillus pabuli E1 genome revealed the presence of 372 genes related to Carbohydrate-Active enzymes (CAZymes), with 98 of them associated with NSPs degrading enzymes that target cellulose, hemicellulose, and pectin. Additionally, although lignin is not an NSP, two lignin-degrading enzymes were also examined because the presence of lignin alongside NSPs can hinder the catalytic effect of enzymes on NSPs. To confirm the catalytic ability of the degrading enzymes, an in vitro enzyme activity assay was conducted. The results demonstrated that the endoglucanase activity reached 5.37 U/mL, while beta-glucosidase activity was 4.60 U/mL. The filter paper experiments did not detect any reducing sugars. The xylanase and beta-xylosidase activities were measured at 11.05 and 4.16 U/mL, respectively. Furthermore, the pectate lyase and pectin lyase activities were found to be 8.19 and 2.43 U/mL, respectively. The activities of laccase and MnP were determined as 1.87 and 4.30 U/mL, respectively. The researchers also investigated the effect of P. pabuli E1 on the degradation of NSPs through the solid-state fermentation of DDGS. After 240 h of fermentation, the results showed degradation rates of 11.86% for hemicellulose, 11.53% for cellulose, and 8.78% for lignin. Moreover, the crude protein (CP) content of DDGS increased from 26.59% to 30.59%. In conclusion, this study demonstrated that P. pabuli E1 possesses various potential NSPs degrading enzymes that can effectively eliminate NSPs in feed. This process improves the quality and availability of the feed, which is important for animal farming as it seeks alternative protein sources to replace traditional nutrients.

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Pectin lyase overproduction by Penicillium griseoroseum mutants resistant to catabolite repression

Cited by 13 publications

References 34 publications

Microbial Pectinases: A Review on Molecular and Biotechnological Perspectives

Microbial Pectinases: A Review on Molecular and Biotechnological Perspectives

Characterization of yeast mutant strains for starter culture in Arabica coffee fermentation

Feasibility insights into the application of Paenibacillus pabuli E1 in animal feed to eliminate non-starch polysaccharides

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