Reaction mechanism of β-apiosidase from Aspergillus aculeatus
•Reaction mechanism of apiosidase was studied by 1H NMR.•Apiosidase in Viscozyme L is inverting glycosidase.•Viscozyme L does not catalyze transapiosylations. Apiosidases are glycosidases relevant for aroma development during fermentation of wines and black tea. Reaction mechanism of apiosidase from...
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| Veröffentlicht in: | Food chemistry 2019-02, Vol.274, p.543-546 |
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| container_title | Food chemistry |
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| creator | Mastihuba, Vladimír Karnišová Potocká, Elena Uhliariková, Iveta Kis, Peter Kozmon, Stanislav Mastihubová, Mária |
| description | •Reaction mechanism of apiosidase was studied by 1H NMR.•Apiosidase in Viscozyme L is inverting glycosidase.•Viscozyme L does not catalyze transapiosylations.
Apiosidases are glycosidases relevant for aroma development during fermentation of wines and black tea. Reaction mechanism of apiosidase from Aspergillus aculeatus in commercial glycanase Viscozyme L was studied by 1H NMR technique. Study of hydrolysis of 4-nitrophenyl β-D-apiofuranoside revealed that this reaction proceeds with inversion of hydroxyl group in the anomeric center, which confirms inverting mechanism of the enzyme and its inability to catalyze transapiosylation in syntheses of apiosides. |
| doi_str_mv | 10.1016/j.foodchem.2018.09.003 |
| format | Article |
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Apiosidases are glycosidases relevant for aroma development during fermentation of wines and black tea. Reaction mechanism of apiosidase from Aspergillus aculeatus in commercial glycanase Viscozyme L was studied by 1H NMR technique. Study of hydrolysis of 4-nitrophenyl β-D-apiofuranoside revealed that this reaction proceeds with inversion of hydroxyl group in the anomeric center, which confirms inverting mechanism of the enzyme and its inability to catalyze transapiosylation in syntheses of apiosides.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2018.09.003</identifier><identifier>PMID: 30372976</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Apiosidase ; Aspergillus - enzymology ; Fermentation ; Glucosidases - metabolism ; Glycosides - metabolism ; Hydrolysis ; Inverting glycosidase ; NMR ; Reaction mechanism ; Viscozyme L</subject><ispartof>Food chemistry, 2019-02, Vol.274, p.543-546</ispartof><rights>2018 Elsevier Ltd</rights><rights>Copyright © 2018 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-75bb2c6e62691aeae7b53c922d9b46257a04dc7683b5286c72e196de2213e0163</citedby><cites>FETCH-LOGICAL-c368t-75bb2c6e62691aeae7b53c922d9b46257a04dc7683b5286c72e196de2213e0163</cites><orcidid>0000-0001-8827-0635</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.foodchem.2018.09.003$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30372976$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mastihuba, Vladimír</creatorcontrib><creatorcontrib>Karnišová Potocká, Elena</creatorcontrib><creatorcontrib>Uhliariková, Iveta</creatorcontrib><creatorcontrib>Kis, Peter</creatorcontrib><creatorcontrib>Kozmon, Stanislav</creatorcontrib><creatorcontrib>Mastihubová, Mária</creatorcontrib><title>Reaction mechanism of β-apiosidase from Aspergillus aculeatus</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>•Reaction mechanism of apiosidase was studied by 1H NMR.•Apiosidase in Viscozyme L is inverting glycosidase.•Viscozyme L does not catalyze transapiosylations.
Apiosidases are glycosidases relevant for aroma development during fermentation of wines and black tea. Reaction mechanism of apiosidase from Aspergillus aculeatus in commercial glycanase Viscozyme L was studied by 1H NMR technique. Study of hydrolysis of 4-nitrophenyl β-D-apiofuranoside revealed that this reaction proceeds with inversion of hydroxyl group in the anomeric center, which confirms inverting mechanism of the enzyme and its inability to catalyze transapiosylation in syntheses of apiosides.</description><subject>Apiosidase</subject><subject>Aspergillus - enzymology</subject><subject>Fermentation</subject><subject>Glucosidases - metabolism</subject><subject>Glycosides - metabolism</subject><subject>Hydrolysis</subject><subject>Inverting glycosidase</subject><subject>NMR</subject><subject>Reaction mechanism</subject><subject>Viscozyme L</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtOwzAURS0EoqWwhSpDJgn-JLYzQVQVP6kSEoKx5dgv1FUSFztBYlsshDWRqpQpozc5913dg9Cc4Ixgwq82We29NWtoM4qJzHCZYcyO0JRIwVKBBT1GU8ywTCXJ-QSdxbjBGO_YUzRhmAlaCj5F18-gTe98l7Rg1rpzsU18nXx_pXrrfHRWR0jq4NtkEbcQ3lzTDDHRZmhA90M8Rye1biJc_N4Zer27fVk-pKun-8flYpUaxmWfiqKqqOHAKS-JBg2iKpgpKbVllXNaCI1zawSXrCqo5EZQICW3QClhMM5lM3S5_7sN_n2A2KvWRQNNozvwQ1SUUEFKmY8OZojvURN8jAFqtQ2u1eFTEax27tRGHdypnQ-FSzXmxuD8t2OoWrB_sYOsEbjZAzAu_XAQVDQOOgPWBTC9st791_EDsRmDSg</recordid><startdate>20190215</startdate><enddate>20190215</enddate><creator>Mastihuba, Vladimír</creator><creator>Karnišová Potocká, Elena</creator><creator>Uhliariková, Iveta</creator><creator>Kis, Peter</creator><creator>Kozmon, Stanislav</creator><creator>Mastihubová, Mária</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-8827-0635</orcidid></search><sort><creationdate>20190215</creationdate><title>Reaction mechanism of β-apiosidase from Aspergillus aculeatus</title><author>Mastihuba, Vladimír ; Karnišová Potocká, Elena ; Uhliariková, Iveta ; Kis, Peter ; Kozmon, Stanislav ; Mastihubová, Mária</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-75bb2c6e62691aeae7b53c922d9b46257a04dc7683b5286c72e196de2213e0163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Apiosidase</topic><topic>Aspergillus - enzymology</topic><topic>Fermentation</topic><topic>Glucosidases - metabolism</topic><topic>Glycosides - metabolism</topic><topic>Hydrolysis</topic><topic>Inverting glycosidase</topic><topic>NMR</topic><topic>Reaction mechanism</topic><topic>Viscozyme L</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mastihuba, Vladimír</creatorcontrib><creatorcontrib>Karnišová Potocká, Elena</creatorcontrib><creatorcontrib>Uhliariková, Iveta</creatorcontrib><creatorcontrib>Kis, Peter</creatorcontrib><creatorcontrib>Kozmon, Stanislav</creatorcontrib><creatorcontrib>Mastihubová, Mária</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mastihuba, Vladimír</au><au>Karnišová Potocká, Elena</au><au>Uhliariková, Iveta</au><au>Kis, Peter</au><au>Kozmon, Stanislav</au><au>Mastihubová, Mária</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reaction mechanism of β-apiosidase from Aspergillus aculeatus</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2019-02-15</date><risdate>2019</risdate><volume>274</volume><spage>543</spage><epage>546</epage><pages>543-546</pages><issn>0308-8146</issn><eissn>1873-7072</eissn><abstract>•Reaction mechanism of apiosidase was studied by 1H NMR.•Apiosidase in Viscozyme L is inverting glycosidase.•Viscozyme L does not catalyze transapiosylations.
Apiosidases are glycosidases relevant for aroma development during fermentation of wines and black tea. Reaction mechanism of apiosidase from Aspergillus aculeatus in commercial glycanase Viscozyme L was studied by 1H NMR technique. Study of hydrolysis of 4-nitrophenyl β-D-apiofuranoside revealed that this reaction proceeds with inversion of hydroxyl group in the anomeric center, which confirms inverting mechanism of the enzyme and its inability to catalyze transapiosylation in syntheses of apiosides.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>30372976</pmid><doi>10.1016/j.foodchem.2018.09.003</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0001-8827-0635</orcidid></addata></record> |
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| ispartof | Food chemistry, 2019-02, Vol.274, p.543-546 |
| issn | 0308-8146 1873-7072 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Apiosidase Aspergillus - enzymology Fermentation Glucosidases - metabolism Glycosides - metabolism Hydrolysis Inverting glycosidase NMR Reaction mechanism Viscozyme L |
| title | Reaction mechanism of β-apiosidase from Aspergillus aculeatus |
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