Genome Mining of Non-Conventional Yeasts: Search and Analysis of MAL Clusters and Proteins

Viigand, Katrin; Põšnograjeva, Kristina; Visnapuu, Triinu; Alamäe, Tiina

doi:10.3390/genes9070354

Cited by 12 publications

(31 citation statements)

References 85 publications

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“…Such in silico screens could therefore be useful for identifying brewing‐relevant strains from previously isolated and sequenced strains and also save time and resources that would otherwise be needed for laboratory‐based screenings. There is also the possibility of applying this strategy in the pursuit of wild or nonconventional yeast strains possessing brewing‐relevant characteristics (Viigand, Põšnograveja, Visnapuu, & Alamäe, ).…”

Section: Perspectivesmentioning

confidence: 99%

Bioprospecting for brewers: Exploiting natural diversity for naturally diverse beers

Cubillos

Gibson

Grijalva‐Vallejos

et al. 2019

Yeast

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The burgeoning interest in archaic, traditional, and novel beer styles has coincided with a growing appreciation of the role of yeasts in determining beer character as well as a better understanding of the ecology and biogeography of yeasts. Multiple studies in recent years have highlighted the potential of wild Saccharomyces and non-Saccharomyces yeasts for production of beers with novel flavour profiles and other desirable properties. Yeasts isolated from spontaneously fermented beers as well as from other food systems (wine, bread, and kombucha) have shown promise for brewing application, and there is evidence that such cross-system transfers have occurred naturally in the past. We review here the available literature pertaining to the use of nonconventional yeasts in brewing, with a focus on the origins of these yeasts, including methods of isolation. Practical aspects of utilizing nondomesticated yeasts are discussed, and modern methods to facilitate discovery of yeasts with brewing potential are highlighted.

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Section: Perspectivesmentioning

confidence: 99%

Bioprospecting for brewers: Exploiting natural diversity for naturally diverse beers

Cubillos

Gibson

Grijalva‐Vallejos

et al. 2019

Yeast

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“…When mining the genome of B. adeninivorans [2] for the genes related to maltose hydrolysis, we found two genes encoding intracellular GH13 family proteins. Respective proteins were designated as AG1 and AG2 [12]. In MycoCosm, the AG1 was annotated as a protein similar to maltase Mal1 of Schizosaccharomyces pombe and the AG2 as similar to maltases of filamentous fungi Aspergillus and Penicillium.…”

Section: In Silico Analysis Of Baag2mentioning

confidence: 99%

“…The genome of B. adeninivorans was sequenced in 2014 [2]. 2 of 20 The genes potentially encoding α-glucosidases in the genomes of non-conventional yeasts were analysed in Viigand et al [12]. The genes encoding two putative α-glucosidases designated as AG1 and AG2 were revealed in genome of B. adeninivorans.…”

Section: Introductionmentioning

confidence: 99%

“…The genes encoding two putative α-glucosidases designated as AG1 and AG2 were revealed in genome of B. adeninivorans. In the genomes of most yeasts addressed in Viigand et al [12], the α-glucosidase genes resided in maltose utilization (MAL) clusters, whereas no MAL clusters were detected in B. adeninivorans. α-Glucosidases have been popular objects to study protein evolution and phylogenesis [13][14][15][16], but they also have a biotechnological value.…”

Section: Introductionmentioning

confidence: 99%

“…Both types of enzymes hydrolyze sucrose and a synthetic substrate p-nitrophenyl-α-d-glucopyranoside (pNPG) [15,16,23,24]. At the same time, some yeasts such as Ogataea polymorpha and Scheffersomyces stipitis, have promiscuous maltase-isomaltases that hydrolyze maltose-and isomaltose-like substrates [12,16,25].…”

Section: Introductionmentioning

confidence: 99%

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Characterization of a Maltase from an Early-Diverged Non-Conventional Yeast Blastobotrys adeninivorans

Visnapuu

Meldre

Põšnograjeva

et al. 2019

IJMS

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Genome of an early-diverged yeast Blastobotrys (Arxula) adeninivorans (Ba) encodes 88 glycoside hydrolases (GHs) including two α-glucosidases of GH13 family. One of those, the rna_ARAD1D20130g-encoded protein (BaAG2; 581 aa) was overexpressed in Escherichia coli, purified and characterized. We showed that maltose, other maltose-like substrates (maltulose, turanose, maltotriose, melezitose, malto-oligosaccharides of DP 4‒7) and sucrose were hydrolyzed by BaAG2, whereas isomaltose and isomaltose-like substrates (palatinose, α-methylglucoside) were not, confirming that BaAG2 is a maltase. BaAG2 was competitively inhibited by a diabetes drug acarbose (Ki = 0.8 µM) and Tris (Ki = 70.5 µM). BaAG2 was competitively inhibited also by isomaltose-like sugars and a hydrolysis product—glucose. At high maltose concentrations, BaAG2 exhibited transglycosylating ability producing potentially prebiotic di- and trisaccharides. Atypically for yeast maltases, a low but clearly recordable exo-hydrolytic activity on amylose, amylopectin and glycogen was detected. Saccharomyces cerevisiae maltase MAL62, studied for comparison, had only minimal ability to hydrolyze these polymers, and its transglycosylating activity was about three times lower compared to BaAG2. Sequence identity of BaAG2 with other maltases was only moderate being the highest (51%) with the maltase MalT of Aspergillus oryzae.

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Giant GAL gene clusters for the melibiose‐galactose pathway in Torulaspora

Venkatesh

Murray

Coughlan

et al. 2020

Yeast

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In many yeast species, the three genes at the centre of the galactose catabolism pathway, GAL1, GAL10 and GAL7, are neighbours in the genome and form a metabolic gene cluster. We report here that some yeast strains in the genus Torulaspora have much larger GAL clusters that include genes for melibiase (MEL1), galactose permease (GAL2), glucose transporter (HGT1), phosphoglucomutase (PGM1) and the transcription factor GAL4, in addition to GAL1, GAL10, and GAL7. Together, these eight genes encode almost all the steps in the pathway for catabolism of extracellular melibiose (a disaccharide of galactose and glucose). We show that a progenitor 5‐gene cluster containing GAL 7‐1‐10‐4‐2 was likely present in the common ancestor of Torulaspora and Zygotorulaspora. It added PGM1 and MEL1 in the ancestor of most Torulaspora species. It underwent further expansion in the T. pretoriensis clade, involving the fusion of three progenitor clusters in tandem and the gain of HGT1. These giant GAL clusters are highly polymorphic in structure, and subject to horizontal transfers, pseudogenization and gene losses. We identify recent horizontal transfers of complete GAL clusters from T. franciscae into one strain of T. delbrueckii, and from a relative of T. maleeae into one strain of T. globosa. The variability and dynamic evolution of GAL clusters in Torulaspora indicates that there is strong natural selection on the GAL pathway in this genus.

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Genome Mining of Non-Conventional Yeasts: Search and Analysis of MAL Clusters and Proteins

Cited by 12 publications

References 85 publications

Bioprospecting for brewers: Exploiting natural diversity for naturally diverse beers

Bioprospecting for brewers: Exploiting natural diversity for naturally diverse beers

Characterization of a Maltase from an Early-Diverged Non-Conventional Yeast Blastobotrys adeninivorans

Giant GAL gene clusters for the melibiose‐galactose pathway in Torulaspora

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