Isolation and Characterization of a β-Primeverosidase-Like Enzyme from<i>Penicillium multicolor</i>

Tsuruhami, Kazutaka; Mori, Shigeharu; Amarume, Satoshi; Saruwatari, Shigetaka; Murata, Takeomi; Hirakake, Jun; Sakata, Kanzo; Usui, Taichi

doi:10.1271/bbb.70.691

Cited by 20 publications

(20 citation statements)

References 17 publications

(21 reference statements)

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“…Deglycosylation of these compounds most often involves the sequential action of two β-glycosidases in contrast to the one-step hydrolytic release of the disaccharide moiety from the aglycone by β-diglycosidases [55]. The characterized enzymes are a hesperidin 6-O-α-L-rhamnosyl-β-glucosidase (EC 3.2.1.168) from Stilbella fimetaria from which a partial sequence has been obtained [56] and a reported β-primeverosidase (EC 3.2.1.149) from Penicillium multicolor TS-5 [57]. This subfamily is present in the genera Aspergillus and Penicillium known for interaction with plants.…”

Section: Resultsmentioning

confidence: 99%

Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)

et al. 2012

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BackgroundThe large Glycoside Hydrolase family 5 (GH5) groups together a wide range of enzymes acting on β-linked oligo- and polysaccharides, and glycoconjugates from a large spectrum of organisms. The long and complex evolution of this family of enzymes and its broad sequence diversity limits functional prediction. With the objective of improving the differentiation of enzyme specificities in a knowledge-based context, and to obtain new evolutionary insights, we present here a new, robust subfamily classification of family GH5.ResultsAbout 80% of the current sequences were assigned into 51 subfamilies in a global analysis of all publicly available GH5 sequences and associated biochemical data. Examination of subfamilies with catalytically-active members revealed that one third are monospecific (containing a single enzyme activity), although new functions may be discovered with biochemical characterization in the future. Furthermore, twenty subfamilies presently have no characterization whatsoever and many others have only limited structural and biochemical data. Mapping of functional knowledge onto the GH5 phylogenetic tree revealed that the sequence space of this historical and industrially important family is far from well dispersed, highlighting targets in need of further study. The analysis also uncovered a number of GH5 proteins which have lost their catalytic machinery, indicating evolution towards novel functions.ConclusionOverall, the subfamily division of GH5 provides an actively curated resource for large-scale protein sequence annotation for glycogenomics; the subfamily assignments are openly accessible via the Carbohydrate-Active Enzyme database at http://www.cazy.org/GH5.html.

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Section: Resultsmentioning

confidence: 99%

Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)

et al. 2012

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“…Interestingly, the cloned rutinosidase gene with its sequence accession number CAK39791 has been assigned in the CAZy database to the class 5-subfamily 23 of glycoside hydrolases, [16] together with the characterized b-primeverosidase from Penicillium multicolor TS-5 (EC 3.2.1.149; BAG70961) [17] and 7 more fungal enzymes. Significantly more information, including one tertiary [18] and several primary structures, is available on primeverosidases.…”

Section: Expression and Purification Of Recombinant Rutinosidasementioning

confidence: 99%

“…The alignment of these protein sequences with the sequence of the primeverosidase whose structure has been determined (BAC78656) [17] revealed 9 conserved residues (composed of F, G, H, S, T, V, W and Y). However, no clear indication of catalytically important residues could be found.…”

Section: Expression and Purification Of Recombinant Rutinosidasementioning

confidence: 99%

α‐L‐Rhamnosyl‐β‐D‐glucosidase (Rutinosidase) from Aspergillus niger: Characterization and Synthetic Potential of a Novel Diglycosidase

et al. 2014

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Abstract:We report the first heterologous production of a fungal rutinosidase (6-O-a-l-rhamnopyranosyl-b-d-glucopyranosidase) in Pichia pastoris. The recombinant rutinosidase was purified from the culture medium to apparent homogeneity and biochemically characterized. The enzyme reacts with rutin and cleaves the glycosidic linkage between the disaccharide rutinose and the aglycone. Furthermore, it exhibits high transglycosylation activity, transferring rutinose from rutin as a glycosyl donor onto various alcohols and phenols. The utility of the recombinant rutinosidase was demonstrated by its use for the synthesis of a broad spectrum of rutinosides of primary (saturated and unsaturated), secondary, acyclic and phenolic alcohols as well as for the preparation of free rutinose. Moreover, the a-l-rhamnosidase-catalyzed synthesis of a chromogenic substrate for a rutinosidase assay -para-nitrophenyl b-rutinoside -is described.

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“…This is a large group of biologically important enzymes, both biomedical and industrial, which are found in plants and microorganisms, mainly yeasts, and filamentous fungi (Pogorzelski and Wilkowska, 2007). Although, endogenous glycosidic activities increased in the fruit during the ripening process, no evidence of their relationship with the hydrolysis of glycosylated precursors of volatile compounds has been proved so far (Lecas et al, 1991; Kumar and Ramón, 1996; Manzanares et al, 2001; Mizutani et al, 2002; Sarry and Günata, 2004; Wei et al, 2004; Tsuruhami et al, 2006). …”

Section: Introductionmentioning

confidence: 99%

Gene-Metabolite Networks of Volatile Metabolism in Airen and Tempranillo Grape Cultivars Revealed a Distinct Mechanism of Aroma Bouquet Production

Rambla

Trapero-Mozos

Diretto³

et al. 2016

Front. Plant Sci.

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Volatile compounds are the major determinants of aroma and flavor in both grapes and wine. In this study, we investigated the emission of volatile and non-volatile compounds during berry maturation in two grape varieties (Airén and Tempranillo) throughout 2010 and 2011. HS-SPME coupled to gas chromatography and mass spectrometry was applied for the identification and relative quantitation of these compounds. Principal component analysis was performed to search for variability between the two cultivars and evolution during 10 developmental stages. Results showed that there are distinct differences in volatile compounds between cultivars throughout fruit development. Early stages were characterized in both cultivars by higher levels of some apocarotenoids such as β-cyclocitral or β-ionone, terpenoids (E)-linalool oxide and (Z)-linalool oxide and several furans, while the final stages were characterized by the highest amounts of ethanol, benzenoid phenylacetaldehyde and 2-phenylethanol, branched-amino acid-derived 3-methylbutanol and 2-methylbutanol, and a large number of lipid derivatives. Additionally, we measured the levels of the different classes of volatile precursors by using liquid chromatography coupled to high resolution mass spectrometry. In both varieties, higher levels of carotenoid compounds were detected in the earlier stages, zeaxanthin and α-carotene were only detected in Airén while neoxanthin was found only in Tempranillo; more variable trends were observed in the case of the other volatile precursors. Furthermore, we monitored the expression of homolog genes of a set of transcripts potentially involved in the biosynthesis of these metabolites, such as some glycosyl hydrolases family 1, lipoxygenases, alcohol dehydrogenases hydroperoxide lyases, O-methyltransferases and carotenoid cleavage dioxygenases during the defined developmental stages. Finally, based on Pearson correlation analyses, we explored the metabolite-metabolite fluctuations within VOCs/precursors during the berry development; as well as tentatively linking the formation of some metabolites detected to the expression of some of these genes. Our data showed that the two varieties displayed a very different pattern of relationships regarding the precursor/volatile metabolite-metabolite fluctuations, being the lipid and the carotenoid metabolism the most distinctive between the two varieties. Correlation analysis showed a higher degree of overall correlation in precursor/volatile metabolite-metabolite levels in Airén, confirming the enriched aroma bouquet characteristic of the white varieties.

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Isolation and Characterization of a β-Primeverosidase-Like Enzyme fromPenicillium multicolor

Cited by 20 publications

References 17 publications

Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)

Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)

α‐L‐Rhamnosyl‐β‐D‐glucosidase (Rutinosidase) from Aspergillus niger: Characterization and Synthetic Potential of a Novel Diglycosidase

Gene-Metabolite Networks of Volatile Metabolism in Airen and Tempranillo Grape Cultivars Revealed a Distinct Mechanism of Aroma Bouquet Production

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