Peculiarities and systematics of microbial diglycosidases, and their applications in food technology
Abstract 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...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Baglioni, Micaela [verfasserIn] Breccia, Javier D. [verfasserIn] Mazzaferro, Laura S. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2021 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Berlin : Springer, 1975, 105(2021), 7 vom: 21. März, Seite 2693-2700 |
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| Übergeordnetes Werk: |
volume:105 ; year:2021 ; number:7 ; day:21 ; month:03 ; pages:2693-2700 |
| Links: |
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| DOI / URN: |
10.1007/s00253-021-11219-9 |
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| Katalog-ID: |
SPR043643655 |
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| 245 | 1 | 0 | |a Peculiarities and systematics of microbial diglycosidases, and their applications in food technology |
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| 520 | |a Abstract 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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| 700 | 1 | |a Mazzaferro, Laura S. |e verfasserin |4 aut | |
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10.1007/s00253-021-11219-9 doi (DE-627)SPR043643655 (DE-599)SPRs00253-021-11219-9-e (SPR)s00253-021-11219-9-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Baglioni, Micaela verfasserin aut Peculiarities and systematics of microbial diglycosidases, and their applications in food technology 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 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. β-primeverosidase (dpeaa)DE-He213 Hesperidin 6- (dpeaa)DE-He213 -α- (dpeaa)DE-He213 -rhamnosyl-β- (dpeaa)DE-He213 -glucosidase (dpeaa)DE-He213 β-rutinosidase (dpeaa)DE-He213 Rutin (dpeaa)DE-He213 Hesperidin (dpeaa)DE-He213 Breccia, Javier D. verfasserin aut Mazzaferro, Laura S. verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 105(2021), 7 vom: 21. März, Seite 2693-2700 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:105 year:2021 number:7 day:21 month:03 pages:2693-2700 https://dx.doi.org/10.1007/s00253-021-11219-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 105 2021 7 21 03 2693-2700 |
| spelling |
10.1007/s00253-021-11219-9 doi (DE-627)SPR043643655 (DE-599)SPRs00253-021-11219-9-e (SPR)s00253-021-11219-9-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Baglioni, Micaela verfasserin aut Peculiarities and systematics of microbial diglycosidases, and their applications in food technology 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 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. β-primeverosidase (dpeaa)DE-He213 Hesperidin 6- (dpeaa)DE-He213 -α- (dpeaa)DE-He213 -rhamnosyl-β- (dpeaa)DE-He213 -glucosidase (dpeaa)DE-He213 β-rutinosidase (dpeaa)DE-He213 Rutin (dpeaa)DE-He213 Hesperidin (dpeaa)DE-He213 Breccia, Javier D. verfasserin aut Mazzaferro, Laura S. verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 105(2021), 7 vom: 21. März, Seite 2693-2700 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:105 year:2021 number:7 day:21 month:03 pages:2693-2700 https://dx.doi.org/10.1007/s00253-021-11219-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 105 2021 7 21 03 2693-2700 |
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10.1007/s00253-021-11219-9 doi (DE-627)SPR043643655 (DE-599)SPRs00253-021-11219-9-e (SPR)s00253-021-11219-9-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Baglioni, Micaela verfasserin aut Peculiarities and systematics of microbial diglycosidases, and their applications in food technology 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 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. β-primeverosidase (dpeaa)DE-He213 Hesperidin 6- (dpeaa)DE-He213 -α- (dpeaa)DE-He213 -rhamnosyl-β- (dpeaa)DE-He213 -glucosidase (dpeaa)DE-He213 β-rutinosidase (dpeaa)DE-He213 Rutin (dpeaa)DE-He213 Hesperidin (dpeaa)DE-He213 Breccia, Javier D. verfasserin aut Mazzaferro, Laura S. verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 105(2021), 7 vom: 21. März, Seite 2693-2700 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:105 year:2021 number:7 day:21 month:03 pages:2693-2700 https://dx.doi.org/10.1007/s00253-021-11219-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 105 2021 7 21 03 2693-2700 |
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10.1007/s00253-021-11219-9 doi (DE-627)SPR043643655 (DE-599)SPRs00253-021-11219-9-e (SPR)s00253-021-11219-9-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Baglioni, Micaela verfasserin aut Peculiarities and systematics of microbial diglycosidases, and their applications in food technology 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 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. β-primeverosidase (dpeaa)DE-He213 Hesperidin 6- (dpeaa)DE-He213 -α- (dpeaa)DE-He213 -rhamnosyl-β- (dpeaa)DE-He213 -glucosidase (dpeaa)DE-He213 β-rutinosidase (dpeaa)DE-He213 Rutin (dpeaa)DE-He213 Hesperidin (dpeaa)DE-He213 Breccia, Javier D. verfasserin aut Mazzaferro, Laura S. verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 105(2021), 7 vom: 21. März, Seite 2693-2700 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:105 year:2021 number:7 day:21 month:03 pages:2693-2700 https://dx.doi.org/10.1007/s00253-021-11219-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 105 2021 7 21 03 2693-2700 |
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10.1007/s00253-021-11219-9 doi (DE-627)SPR043643655 (DE-599)SPRs00253-021-11219-9-e (SPR)s00253-021-11219-9-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Baglioni, Micaela verfasserin aut Peculiarities and systematics of microbial diglycosidases, and their applications in food technology 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract 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. β-primeverosidase (dpeaa)DE-He213 Hesperidin 6- (dpeaa)DE-He213 -α- (dpeaa)DE-He213 -rhamnosyl-β- (dpeaa)DE-He213 -glucosidase (dpeaa)DE-He213 β-rutinosidase (dpeaa)DE-He213 Rutin (dpeaa)DE-He213 Hesperidin (dpeaa)DE-He213 Breccia, Javier D. verfasserin aut Mazzaferro, Laura S. verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 105(2021), 7 vom: 21. März, Seite 2693-2700 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:105 year:2021 number:7 day:21 month:03 pages:2693-2700 https://dx.doi.org/10.1007/s00253-021-11219-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 105 2021 7 21 03 2693-2700 |
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β-primeverosidase Hesperidin 6- -α- -rhamnosyl-β- -glucosidase β-rutinosidase Rutin Hesperidin |
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Baglioni, Micaela @@aut@@ Breccia, Javier D. @@aut@@ Mazzaferro, Laura S. @@aut@@ |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR043643655</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519120442.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">210330s2021 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s00253-021-11219-9</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR043643655</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)SPRs00253-021-11219-9-e</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s00253-021-11219-9-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="q">ASE</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">58.30</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">42.30</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Baglioni, Micaela</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Peculiarities and systematics of microbial diglycosidases, and their applications in food technology</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2021</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract 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. 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|
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Baglioni, Micaela |
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Baglioni, Micaela ddc 570 bkl 58.30 bkl 42.30 misc β-primeverosidase misc Hesperidin 6- misc -α- misc -rhamnosyl-β- misc -glucosidase misc β-rutinosidase misc Rutin misc Hesperidin Peculiarities and systematics of microbial diglycosidases, and their applications in food technology |
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570 ASE 58.30 bkl 42.30 bkl Peculiarities and systematics of microbial diglycosidases, and their applications in food technology β-primeverosidase (dpeaa)DE-He213 Hesperidin 6- (dpeaa)DE-He213 -α- (dpeaa)DE-He213 -rhamnosyl-β- (dpeaa)DE-He213 -glucosidase (dpeaa)DE-He213 β-rutinosidase (dpeaa)DE-He213 Rutin (dpeaa)DE-He213 Hesperidin (dpeaa)DE-He213 |
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ddc 570 bkl 58.30 bkl 42.30 misc β-primeverosidase misc Hesperidin 6- misc -α- misc -rhamnosyl-β- misc -glucosidase misc β-rutinosidase misc Rutin misc Hesperidin |
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ddc 570 bkl 58.30 bkl 42.30 misc β-primeverosidase misc Hesperidin 6- misc -α- misc -rhamnosyl-β- misc -glucosidase misc β-rutinosidase misc Rutin misc Hesperidin |
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ddc 570 bkl 58.30 bkl 42.30 misc β-primeverosidase misc Hesperidin 6- misc -α- misc -rhamnosyl-β- misc -glucosidase misc β-rutinosidase misc Rutin misc Hesperidin |
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Baglioni, Micaela |
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Baglioni, Micaela Breccia, Javier D. Mazzaferro, Laura S. |
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peculiarities and systematics of microbial diglycosidases, and their applications in food technology |
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Peculiarities and systematics of microbial diglycosidases, and their applications in food technology |
| abstract |
Abstract 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. |
| abstractGer |
Abstract 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. |
| abstract_unstemmed |
Abstract 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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| container_issue |
7 |
| title_short |
Peculiarities and systematics of microbial diglycosidases, and their applications in food technology |
| url |
https://dx.doi.org/10.1007/s00253-021-11219-9 |
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| author2 |
Breccia, Javier D. Mazzaferro, Laura S. |
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Breccia, Javier D. Mazzaferro, Laura S. |
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| doi_str |
10.1007/s00253-021-11219-9 |
| up_date |
2024-07-03T19:58:34.341Z |
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| score |
7.4015484 |