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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Main Authors: N.V. Borzova, O. V., Gudzenko, L. D. Varbanets
Format: Article
Language:English
Published: National Academy of Sciences of Ukraine and Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine. 2018-10-01
Series:Biotechnologia Acta
Subjects:
Online Access:http://biotechnology.kiev.ua/images/storage/5_2018/borzova_5_2018.pdf
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spelling 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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