A novel pectin‐degrading enzyme complex from <i>Aspergillus sojae</i><scp>ATCC</scp> 20235 mutants

Mata-Gómez, Marco A.; Heerd, Doreen; Oyanguren-García, Iñigo; Barbero, Francis; Rito‐Palomares, Marco; Fernández‐Lahore, Marcelo

doi:10.1002/jsfa.6864

Cited by 9 publications

(10 citation statements)

References 31 publications

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“…Carbohydrate-Active enZymes (CAZymes) are essential for what carbon sources a species can degrade and utilize. Within section Flavi the CAZymes/carbon utilization is mainly described for A. oryzae 1,2,40 and to a lesser extent for A. flavus [41][42][43][44][45] and A. sojae 46,47 , while only incidental studies have been performed with other species of this group [48][49][50][51][52][53][54] , often describing production or characterization of a certain CAZyme activity or protein, respectively.…”

Section: Resultsmentioning

confidence: 99%

A comparative genomics study of 23 Aspergillus species from section Flavi

et al. 2020

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Section Flavi encompasses both harmful and beneficial Aspergillus species, such as Aspergillus oryzae, used in food fermentation and enzyme production, and Aspergillus flavus, food spoiler and mycotoxin producer. Here, we sequence 19 genomes spanning section Flavi and compare 31 fungal genomes including 23 Flavi species. We reassess their phylogenetic relationships and show that the closest relative of A. oryzae is not A. flavus, but A. minisclerotigenes or A. aflatoxiformans and identify high genome diversity, especially in sub-telomeric regions. We predict abundant CAZymes (598 per species) and prolific secondary metabolite gene clusters (73 per species) in section Flavi. However, the observed phenotypes (growth characteristics, polysaccharide degradation) do not necessarily correlate with inferences made from the predicted CAZyme content. Our work, including genomic analyses, phenotypic assays, and identification of secondary metabolites, highlights the genetic and metabolic diversity within section Flavi.

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Section: Resultsmentioning

confidence: 99%

A comparative genomics study of 23 Aspergillus species from section Flavi

et al. 2020

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“…Moreover, through classic mutagenesis screening strategies based on physical (ultraviolet irradiation) and chemical mutagens, pectinase titers of descending mutants of A. sojae have been improved in SmF and SSF (Heerd et al 2014b ). The potential of some of these high-yield pectinase mutants has been further explored by measuring various pectinase activities including exo-/endo-polygalacturonase (exo-PG/endo-PG), exo-polymethylgalacturonase (exo-PMG), and pectin lyase using two different carbon sources in SSF (Mata-Gomez et al 2014 ). Recently, an Agrobacterium tumefaciens -mediated transformation (ATMT) method was described for A. sojae , and heterologous expression of the enhanced green fluorescent protein (EGFP) was demonstrated successfully (Mora-Lugo et al 2014 ).…”

Section: Introductionmentioning

confidence: 99%

Improved biomass and protein production in solid-state cultures of an Aspergillus sojae strain harboring the Vitreoscilla hemoglobin

Mora-Lugo

Madrigal

Yelemane

et al. 2015

Appl Microbiol Biotechnol

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The biotechnological value of Aspergillus sojae ATCC 20235 (A. sojae) for production of pectinases in solid-state fermentation (SSF) has been demonstrated recently. However, a common drawback of fungal solid-state cultures is the poor diffusion of oxygen into the fungi that limits its growth and biological productivity. The bacterial Vitreoscilla hemoglobin (VHb) has favored the metabolism and productivities of various bacterial and yeast strains besides alleviating hypoxic conditions of its native host, but the use of VHb in filamentous fungi still remains poor explored. Based on the known effects of VHb, this study assessed its applicability to improve A. sojae performance in SSF. The VHb gene (vgb) under control of the constitutive Aspergillus nidulants gpdA promoter was introduced into the genome of A. sojae by Agrobacterium-mediated transformation. Successful fungal transformants were identified by fluorescence microscopy and polymerase chain reaction (PCR) analyses. In solid-state cultures, the content of protease, exo-polygalacturonase (exo-PG), and exo-polymethylgalacturonase (exo-PMG) of the transformed fungus (A. sojae vgb+) improved were 26, 60, and 44 % higher, respectively, in comparison to its parental strain (A. sojae wt). Similarly, biomass content was also 1.3 times higher in the transformant strain. No significant difference was observed in endo-polygalacturonase (endo-PG) content between both fungal strains, suggesting dissimilar effects of VHb towards different enzymatic productions. Overall, our results show that biomass, protease, and exo-pectinase content of A. sojae in SSF can be improved by transformation with VHb.

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“…This increase can be attributed to the action of other pectin‐degrading enzymes present in the CE, which were described by Mata‐Gómez et al . (), that may contribute to degrade pectin besides PG, thereby contributing to the release of phenolic compounds from tissue to grape mash. Besides, some other pectin‐degrading activities such as β‐glucosidase, xylanase, cellulose, α‐ and β‐galactosidase and arabinofuranosidase have been found in the crude extract from the A. sojae mutant (data not shown).…”

Section: Resultsmentioning

confidence: 97%

“…The significant increase by CE is probably raised from other possible pectin‐degrading enzymes present in CE, and not in the semi‐purified preparations, that may also act on pectin as described by Mata‐Gómez et al . (). No significant differences were found for CDs of macerated grape mash among treatments (Table ).…”

Section: Resultsmentioning

confidence: 97%

Partial purification of a polygalacturonase from a new Aspergillus sojae mutant and its application in grape mash maceration

Yıldız

Mata-Gómez

Tarı

et al. 2017

Int J of Food Sci Tech

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Summary The use of polygalacturonase (PG) preparations in winemaking promotes the release of phenolic compounds. A PG from a new source, Aspergillus sojae mutant, was semi‐purified and tested for grape mash maceration. Crude extract (CE), a commercial pectinase, and two high PG activity semi‐purified preparations, FI and FII, were applied for maceration at PG activity of 3.5 U g−1 of grape for 46 h. Enzyme‐assisted maceration significantly (P < 0.05) increased the total phenolic content from 255.8 to 916.3 ± 5.2, 5732.9 ± 9.9, 563.4 ± 6.7 and 620.6 ± 18.4 mg L−1 for CE, commercial pectinase, FI and FII, respectively. The content of individual phenolics such as gallic, protocatechuic, chlorogenic and p‐coumaric acids was improved. Principal component and hierarchical clustering analyses suggested that CE has a better performance upon the release of phenols. Semi‐purified preparations acted similar to commercial pectinase. These findings open an opportunity for the potential use of PG from the mutant strain as an alternative macerating enzyme.

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A novel pectin‐degrading enzyme complex from Aspergillus sojaeATCC 20235 mutants

Abstract: Mutant M3 was the best PDE producer using sugar beet. Mutant strains presented a PDE complex featuring high endo-PG and very low PE activities. This novel complex with low de-esterifying activity can be exploited in the food industry to degrade pectin without releasing methanol.

Cited by 9 publications

References 31 publications

A comparative genomics study of 23 Aspergillus species from section Flavi

A comparative genomics study of 23 Aspergillus species from section Flavi

Improved biomass and protein production in solid-state cultures of an Aspergillus sojae strain harboring the Vitreoscilla hemoglobin

Partial purification of a polygalacturonase from a new Aspergillus sojae mutant and its application in grape mash maceration

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