DEGRADATION OF FLAVONOIDS BY Cryptococcus albidus α-L-RHAMNOSIDASE
The aim of the work was to investigate the possibility of practical use substrate specificity of α-Lrhamnosidase Cryptococcus albidus. p-Nitrophenyl derivatives of monosaccharides were used to determine the activity and specificity of the enzyme. The ability to hydrolyze of natural substrates was ev...
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National Academy of Sciences of Ukraine and Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine.
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doaj-3534acf5047f4f759878c66ac13e07442020-11-24T21:09:57ZengNational Academy of Sciences of Ukraine and Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine.Biotechnologia Acta2410-776X2410-776X2018-10-01115354110.15407/biotech11.05.035DEGRADATION OF FLAVONOIDS BY Cryptococcus albidus α-L-RHAMNOSIDASE N.V. Borzova0O. V., Gudzenko1L. D. Varbanets2Zabolotny Institute of Microbiology and Virology of the National Academy of Sciences of Ukraine, KyivZabolotny Institute of Microbiology and Virology of the National Academy of Sciences of Ukraine, KyivZabolotny Institute of Microbiology and Virology of the National Academy of Sciences of Ukraine, KyivThe aim of the work was to investigate the possibility of practical use substrate specificity of α-Lrhamnosidase Cryptococcus albidus. p-Nitrophenyl derivatives of monosaccharides were used to determine the activity and specificity of the enzyme. The ability to hydrolyze of natural substrates was evaluated by Davis and high-performance liquid chromatography methods. It was shown that the enzyme exhibits narrow specificity towards the glycon of synthetic substrates and hydrolyzes only p-nitrophenyl-α-L-rhamnopyranoside (Km 4.5 mM) and p-nitrophenyl-α-D-glucopyranoside (Km 10.0 mM). C. albidus α-L-rhamnosidase the most active degrades naringin (Km 0.77 mM), releasing prunin and naringenin. Km for neohesperidin was 3.3 mM. The efficacy of the naringin hydrolysis in grapefruit and pomelo juice was 98 and 94% in 60 min (40 оC, 2 U/ml). As the result of treatment by α -L-rhamnosidase of green tea and orange juice, there was a decrease in the content of rutin, narirutin and hesperidin, indicating that the α -1,2- and α -1,6-linked rhamnose can be cleaved from natural flavonoids. Thus, the study shows the efficiency of treating citrus juices and green tea with C. albidus α -L-rhamnosidase for the purpose of improving their taste qualities and obtaining bioavailable flavonoids glucosides.http://biotechnology.kiev.ua/images/storage/5_2018/borzova_5_2018.pdfspecificity of Cryptococcus albidusα-L-rhamnosidasespecificity naringinneohesperidinrutinflavonoidscitrus juicesgreen tea. |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
N.V. Borzova O. V., Gudzenko L. D. Varbanets |
spellingShingle |
N.V. Borzova O. V., Gudzenko L. D. Varbanets DEGRADATION OF FLAVONOIDS BY Cryptococcus albidus α-L-RHAMNOSIDASE Biotechnologia Acta specificity of Cryptococcus albidus α-L-rhamnosidase specificity naringin neohesperidin rutin flavonoids citrus juices green tea. |
author_facet |
N.V. Borzova O. V., Gudzenko L. D. Varbanets |
author_sort |
N.V. Borzova |
title |
DEGRADATION OF FLAVONOIDS BY Cryptococcus albidus α-L-RHAMNOSIDASE |
title_short |
DEGRADATION OF FLAVONOIDS BY Cryptococcus albidus α-L-RHAMNOSIDASE |
title_full |
DEGRADATION OF FLAVONOIDS BY Cryptococcus albidus α-L-RHAMNOSIDASE |
title_fullStr |
DEGRADATION OF FLAVONOIDS BY Cryptococcus albidus α-L-RHAMNOSIDASE |
title_full_unstemmed |
DEGRADATION OF FLAVONOIDS BY Cryptococcus albidus α-L-RHAMNOSIDASE |
title_sort |
degradation of flavonoids by cryptococcus albidus α-l-rhamnosidase |
publisher |
National Academy of Sciences of Ukraine and Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine. |
series |
Biotechnologia Acta |
issn |
2410-776X 2410-776X |
publishDate |
2018-10-01 |
description |
The aim of the work was to investigate the possibility of practical use substrate specificity of α-Lrhamnosidase Cryptococcus albidus. p-Nitrophenyl derivatives of monosaccharides were used to determine the activity and specificity of the enzyme. The ability to hydrolyze of natural substrates was evaluated by Davis and high-performance liquid chromatography methods. It was shown that the enzyme exhibits narrow specificity towards the glycon of synthetic substrates and hydrolyzes only p-nitrophenyl-α-L-rhamnopyranoside (Km 4.5 mM) and p-nitrophenyl-α-D-glucopyranoside (Km 10.0 mM). C. albidus α-L-rhamnosidase the most active degrades naringin (Km 0.77 mM), releasing prunin and naringenin. Km for neohesperidin was 3.3 mM. The efficacy of the naringin hydrolysis in grapefruit and pomelo juice was 98 and 94% in 60 min (40 оC, 2 U/ml). As the result of treatment by α -L-rhamnosidase of green tea and orange juice, there was a decrease in the content of rutin, narirutin and hesperidin, indicating that the α -1,2- and α -1,6-linked rhamnose can be cleaved from natural flavonoids. Thus, the study shows the efficiency of treating citrus juices and green tea with C. albidus α -L-rhamnosidase for the purpose of improving their taste qualities and obtaining bioavailable flavonoids glucosides. |
topic |
specificity of Cryptococcus albidus α-L-rhamnosidase specificity naringin neohesperidin rutin flavonoids citrus juices green tea. |
url |
http://biotechnology.kiev.ua/images/storage/5_2018/borzova_5_2018.pdf |
work_keys_str_mv |
AT nvborzova degradationofflavonoidsbycryptococcusalbidusalrhamnosidase AT ovgudzenko degradationofflavonoidsbycryptococcusalbidusalrhamnosidase AT ldvarbanets degradationofflavonoidsbycryptococcusalbidusalrhamnosidase |
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1716756917092614144 |