Reaction mechanism of β-apiosidase from Aspergillus aculeatus

Mastihuba, Vladimı́r; Potocká, Elena Karnišová; Uhliariková, Iveta; Kis, Peter; Kozmon, Stanislav; Mastihubová, Mária

doi:10.1016/j.foodchem.2018.09.003

Cited by 8 publications

(7 citation statements)

References 26 publications

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“…Table 2 summarizes molecular and catalytic properties of purified apiosidases. Mastihuba et al [31] studied the reaction mechanism of β-apiofuranosidase from Aspergillus aculeatus in commercial glycanase Viscozyme L and revealed that hydrolysis of pNP β-D-apiofuranoside proceeds with the inversion of the configuration of hydroxyl in the anomeric center. Since crystal structures and molecular biology of purified enzymes are still unavailable, further research work is required to fully understand the molecular mechanism of catalysis by this enzyme.…”

Section: Purification and Characterization Of Apiosidasesmentioning

confidence: 99%

“…Many exo-acting β-apiosidases were able to hydrolyse 4-nitrophenyl (pNP) β-D-apiofuranoside in screenings. Synthetic pNP β-D-apiofuranoside was successfully used for spectrophotometric analysis of liberated nitrophenol (Figure 4), [22,23,26,27,31]. The assay protocols vary in details such as substrate concentration, type and pH of the buffer, the way of stopping of the substrate hydrolysis or reaction time.…”

Section: Substrate Specificity and Assaying Of β-Apiosidasesmentioning

confidence: 99%

“…Direct glycosidase-driven apiosylation of free aglycones or simple glycosides is however hampered by the practical unavailability of retaining apiosidases. A very recent study of β-apiosidase from Aspergillus aculeatus revealed its inverting reaction mechanism [31]. The inverting glycosidases are unable to catalyze transglycosylations and can form a glycosidic bond only by reverse hydrolysis starting from free monosaccharide.…”

Section: Potential Applications Of Apiose-relevant Glycosidasesmentioning

confidence: 99%

“…This anomer stands for ca. 30% of all anomeric forms present in the equilibrated solution of free apiose [31]. Most of the identified β-apiosidases are produced by the genus Aspergillus [22,[26][27][28]; it is therefore probable that the enzymes are working under the same inverting mechanism.…”

Section: Potential Applications Of Apiose-relevant Glycosidasesmentioning

confidence: 99%

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Apiose-Relevant Glycosidases

Potocká¹,

Mastihubová²,

Mastihuba³

2021

Catalysts

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Apiose is a branched pentose naturally occurring either as a component of the plant cell wall polysaccharides or as a sugar moiety present in numerous plant secondary metabolites such as flavonoid and phenylethanoid glycosides, substrates in plant defense systems or as glycosylated aroma precursors. The enzymes catalyzing hydrolysis of such apiosylated substances (mainly glycosidases specific towards apiose or acuminose) have promising applications not only in hydrolysis (flavor development), but potentially also in the synthesis of apiosides and apioglucosides with pharmaceutical relevance. This review summarizes the actual knowledge of glycosidases recognizing apiose and their potential application in biocatalysis.

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Section: Purification and Characterization Of Apiosidasesmentioning

confidence: 99%

Section: Substrate Specificity and Assaying Of β-Apiosidasesmentioning

confidence: 99%

Section: Potential Applications Of Apiose-relevant Glycosidasesmentioning

confidence: 99%

Section: Potential Applications Of Apiose-relevant Glycosidasesmentioning

confidence: 99%

See 2 more Smart Citations

Apiose-Relevant Glycosidases

Potocká¹,

Mastihubová²,

Mastihuba³

2021

Catalysts

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“…(Kis et al, 2016). Reaction mechanism of exo-acting b-apiosidase found in Viscozyme L, a product of Aspergillus aculeatus, has recently been studied in detail by Mastihuba et al (2019). Results obtained from experiments using H NMR spectroscopy revealed the inverting mechanism of the enzyme, which is therefore unable to provide transglycosylation re actions.…”

Section: Introductionmentioning

confidence: 99%

Apiin-induction of β-apiosidase production by Aspergillus sp. strains

Karkeszová

Illeová

Kis

et al. 2020

Acta Chimica Slovaca

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Abstractβ-Apiosidase is a rare glycosidase applied in winemaking for flavour enhancement. This enzyme is involved in the release of volatile terpenes by hydrolysis of their odourless glycosidic precursors. It is found as a minor component in commercial pectinase/cellulase preparations. Microbial production of β-apiosidase by two Aspergillus sp. strains was investigated. Apiin-induced production of this extracellular glycosidase was confirmed only during the cultivation of Aspergillus niger CBS 554.65 but the high productivity value reported in the work of Dupin et al. (1992) J. Agric. Food Chem. 40(10): 1886—1891 could not be reproduced. The achieved productivity was by far not satisfactory considering the apiin cost. Commercial enzyme preparations with β-apiosidase side-activity thus remain a better alternative as the enzyme source for biocatalytic applications.

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Peculiarities and systematics of microbial diglycosidases, and their applications in food technology

Baglioni

Breccia

Mazzaferro

2021

Appl Microbiol Biotechnol

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Diglycosidases are endo-β-glucosidases that hydrolyze the heterosidic linkage of diglycoconjugates, thereby releasing in a single reaction the disaccharide and the aglycone. Plant diglycosidases belong to the glycoside hydrolase family 1 and are associated with defense mechanisms. Microbial diglycosidases exhibit higher diversity-they belong to the families 3, 5, and 55-and play a catabolic role. As diglycoconjugates are widespread in the environments, so are the microbial diglycosidases, which allow their utilization as nutritional source and carbon recycling. In the last 10 years, six microbial diglycosidases have been sequenced, and for two of them, the three-dimensional structure has been elucidated. This knowledge allowed the identification of their diverse phylogenetic origin, and gave insights into the understanding of the substrate specificity. Here, the last advances and the applications of microbial diglycosidases are reviewed. Key points• Substrate specificity and phylogenetic relationships of diglycosidases are reviewed.• On-going and potential applications of diglycosidases are discussed.

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Reaction mechanism of β-apiosidase from Aspergillus aculeatus

Cited by 8 publications

References 26 publications

Apiose-Relevant Glycosidases

Apiose-Relevant Glycosidases

Apiin-induction of β-apiosidase production by Aspergillus sp. strains

Peculiarities and systematics of microbial diglycosidases, and their applications in food technology

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