Modification of native fucoidan from Fucus evanescens by recombinant fucoidanase from marine bacteria Formosa algae

•Enzymatic cleavage of native fucoidan FeF by fucoidanase FFA1 yielded fractions HMP and LMP.•HMP are polymeric fragments of FeF that have a regular structure.•FeF and HMP have anticancer effect on colon cancer cells in vitro.•Anticancer effect of HMP was comparable to the activity of FeF but not id...

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Published in:	Carbohydrate polymers Vol. 193; pp. 189 - 195
Main Authors:	Silchenko, Artem S., Rasin, Anton B., Kusaykin, Mikhail I., Malyarenko, Olesya S., Shevchenko, Natalie M., Zueva, Anastasya O., Kalinovsky, Anatoly I., Zvyagintseva, Tatyana N., Ermakova, Svetlana P.
Format:	Journal Article
Language:	English
Published:	England Elsevier Ltd 01-08-2018
Subjects:	Anticancer activity Antineoplastic Agents - chemistry Antineoplastic Agents - metabolism Antineoplastic Agents - pharmacology Biocatalysis Carbohydrate Conformation Cell Proliferation - drug effects Dose-Response Relationship, Drug Drug Screening Assays, Antitumor Endo-fucoidanase Fucoidan depolymerization Fucoidan from Fucus evanescens Fucoidanase Fucus - chemistry Fucus - enzymology Fucus - metabolism Humans Hydrolases - chemistry Hydrolases - metabolism Marine bacteria Polysaccharides - chemistry Polysaccharides - metabolism Polysaccharides - pharmacology Recombinant Proteins - chemistry Recombinant Proteins - metabolism Structure-Activity Relationship Tumor Cells, Cultured Fucoidanase Fucoidan from Fucus evanescens Fucoidan depolymerization Endo-fucoidanase Anticancer activity Marine bacteria
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Abstract	•Enzymatic cleavage of native fucoidan FeF by fucoidanase FFA1 yielded fractions HMP and LMP.•HMP are polymeric fragments of FeF that have a regular structure.•FeF and HMP have anticancer effect on colon cancer cells in vitro.•Anticancer effect of HMP was comparable to the activity of FeF but not identical. Enzymatic depolymerization of fucoidans attracts many researchers due to the opportunity of obtaining standardized fucoidan fragments. Fucoidanase catalyzes the cleavage of fucoidan from Fucus evanescens (FeF) to form low molecular weight products (LMP) and a polymeric fraction (HMP) with 50.8 kDa molecular weight and more than 50% yield. NMR spectroscopy shows that the HMP fraction has regular structure and consists of a repeating fragment [→3)-α-l-Fucp2,4OSO3−-(1 → 4)-α-l-Fucp2,4OSO3−-(1 → 4)-α-l-Fucp2OSO3−-(1→]n. The anticancer effects of FeF fucoidan and its derivative (HMP) were studied in vitro on colon cancer cells HCT-116, HT-29, and DLD-1. The anticancer activity of the HMP fraction was found to be slightly lower than that of the FeF fucoidan. Research and practical applications of the enzyme include modification of native fucoidans for purposes of regular and easier characterized derivatives acquisition.
AbstractList	•Enzymatic cleavage of native fucoidan FeF by fucoidanase FFA1 yielded fractions HMP and LMP.•HMP are polymeric fragments of FeF that have a regular structure.•FeF and HMP have anticancer effect on colon cancer cells in vitro.•Anticancer effect of HMP was comparable to the activity of FeF but not identical. Enzymatic depolymerization of fucoidans attracts many researchers due to the opportunity of obtaining standardized fucoidan fragments. Fucoidanase catalyzes the cleavage of fucoidan from Fucus evanescens (FeF) to form low molecular weight products (LMP) and a polymeric fraction (HMP) with 50.8 kDa molecular weight and more than 50% yield. NMR spectroscopy shows that the HMP fraction has regular structure and consists of a repeating fragment [→3)-α-l-Fucp2,4OSO3−-(1 → 4)-α-l-Fucp2,4OSO3−-(1 → 4)-α-l-Fucp2OSO3−-(1→]n. The anticancer effects of FeF fucoidan and its derivative (HMP) were studied in vitro on colon cancer cells HCT-116, HT-29, and DLD-1. The anticancer activity of the HMP fraction was found to be slightly lower than that of the FeF fucoidan. Research and practical applications of the enzyme include modification of native fucoidans for purposes of regular and easier characterized derivatives acquisition. Enzymatic depolymerization of fucoidans attracts many researchers due to the opportunity of obtaining standardized fucoidan fragments. Fucoidanase catalyzes the cleavage of fucoidan from Fucus evanescens (FeF) to form low molecular weight products (LMP) and a polymeric fraction (HMP) with 50.8 kDa molecular weight and more than 50% yield. NMR spectroscopy shows that the HMP fraction has regular structure and consists of a repeating fragment [→3)-α-l-Fucp2,4OSO -(1 → 4)-α-l-Fucp2,4OSO -(1 → 4)-α-l-Fucp2OSO -(1→] . The anticancer effects of FeF fucoidan and its derivative (HMP) were studied in vitro on colon cancer cells HCT-116, HT-29, and DLD-1. The anticancer activity of the HMP fraction was found to be slightly lower than that of the FeF fucoidan. Research and practical applications of the enzyme include modification of native fucoidans for purposes of regular and easier characterized derivatives acquisition.
Author	Malyarenko, Olesya S. Rasin, Anton B. Zueva, Anastasya O. Kalinovsky, Anatoly I. Zvyagintseva, Tatyana N. Kusaykin, Mikhail I. Shevchenko, Natalie M. Ermakova, Svetlana P. Silchenko, Artem S.
Author_xml	– sequence: 1 givenname: Artem S. surname: Silchenko fullname: Silchenko, Artem S. email: artem.silchencko@yandex.ru organization: Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 690022, Vladivostok, 159, Prospect 100-let Vladivostoku, Russia1 – sequence: 2 givenname: Anton B. surname: Rasin fullname: Rasin, Anton B. email: abrus__54@mail.ru organization: Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 690022, Vladivostok, 159, Prospect 100-let Vladivostoku, Russia1 – sequence: 3 givenname: Mikhail I. orcidid: 0000-0001-7117-8103 surname: Kusaykin fullname: Kusaykin, Mikhail I. email: mik@piboc.dvo.ru organization: Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 690022, Vladivostok, 159, Prospect 100-let Vladivostoku, Russia1 – sequence: 4 givenname: Olesya S. surname: Malyarenko fullname: Malyarenko, Olesya S. email: vishchuk@mail.ru organization: Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 690022, Vladivostok, 159, Prospect 100-let Vladivostoku, Russia1 – sequence: 5 givenname: Natalie M. surname: Shevchenko fullname: Shevchenko, Natalie M. email: natalyshe@piboc.dvo.ru organization: Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 690022, Vladivostok, 159, Prospect 100-let Vladivostoku, Russia1 – sequence: 6 givenname: Anastasya O. surname: Zueva fullname: Zueva, Anastasya O. email: zstasya95@gmail.com organization: Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 690022, Vladivostok, 159, Prospect 100-let Vladivostoku, Russia1 – sequence: 7 givenname: Anatoly I. surname: Kalinovsky fullname: Kalinovsky, Anatoly I. email: kaaniv@pidoc.dvo.ru organization: Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 690022, Vladivostok, 159, Prospect 100-let Vladivostoku, Russia1 – sequence: 8 givenname: Tatyana N. surname: Zvyagintseva fullname: Zvyagintseva, Tatyana N. email: zvyag@piboc.dvo.ru organization: Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 690022, Vladivostok, 159, Prospect 100-let Vladivostoku, Russia1 – sequence: 9 givenname: Svetlana P. surname: Ermakova fullname: Ermakova, Svetlana P. email: swetlana_e@mail.ru organization: Laboratory of Enzyme Chemistry, G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, 690022, Vladivostok, 159, Prospect 100-let Vladivostoku, Russia1
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Keywords	Fucoidanase Fucoidan from Fucus evanescens Fucoidan depolymerization Endo-fucoidanase Anticancer activity Marine bacteria
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Snippet	•Enzymatic cleavage of native fucoidan FeF by fucoidanase FFA1 yielded fractions HMP and LMP.•HMP are polymeric fragments of FeF that have a regular... Enzymatic depolymerization of fucoidans attracts many researchers due to the opportunity of obtaining standardized fucoidan fragments. Fucoidanase catalyzes...
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SubjectTerms	Anticancer activity Antineoplastic Agents - chemistry Antineoplastic Agents - metabolism Antineoplastic Agents - pharmacology Biocatalysis Carbohydrate Conformation Cell Proliferation - drug effects Dose-Response Relationship, Drug Drug Screening Assays, Antitumor Endo-fucoidanase Fucoidan depolymerization Fucoidan from Fucus evanescens Fucoidanase Fucus - chemistry Fucus - enzymology Fucus - metabolism Humans Hydrolases - chemistry Hydrolases - metabolism Marine bacteria Polysaccharides - chemistry Polysaccharides - metabolism Polysaccharides - pharmacology Recombinant Proteins - chemistry Recombinant Proteins - metabolism Structure-Activity Relationship Tumor Cells, Cultured
Title	Modification of native fucoidan from Fucus evanescens by recombinant fucoidanase from marine bacteria Formosa algae
URI	https://dx.doi.org/10.1016/j.carbpol.2018.03.094 https://www.ncbi.nlm.nih.gov/pubmed/29773371
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