Differential activities of fungi-derived tannases on biotransformation and substrate inhibition in green tea extract

Joo Hyun Baik, Hyung Joo Suh, So Young Cho, Yooheon Park, Hyeon Son Choi

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Tannases are important enzymes in the antioxidant potential of tea leaves. In this study, we evaluated the effect of two tannases (T1 and T2) on biotransformation of tea polyphenols and antioxidative activities from catechins in green tea extract (GTE). The T1 tannase-catalyzed reaction was inhibited by the addition of >2.0% GTE substrate, whereas the T2-catalyzed reaction was not inhibited, even by addition of 5.0% GTE. Furthermore, the T1 tannase-catalyzed reaction was inhibited by addition of 10mgmL<sup>-1</sup> EGCG, whereas the T2 tannase-catalyzed reaction did not display any inhibitory effect. These results indicate that T2 tannase was more tolerant than T1 tannase to substrate inhibition in degallation reactions. Specifically, the substrate EGCG (90,687.1μgmL<sup>-1</sup>) was transformed into gallic acid (50,242.9μgmL<sup>-1</sup>) and EGC (92,598.3μgmL<sup>-1</sup>) after 1-h treatment with T2 tannase (500Ug<sup>-1</sup>). The tannase-mediated product displayed higher in vitro radical-scavenging activity than the control. IC<inf>50</inf> value of GTE on ABTS and DPPH radicals (46.1μgmL<sup>-1</sup> and 18.4μgmL<sup>-1</sup>, respectively) decreased markedly after T2 tannase treatment (to 35.8μgmL<sup>-1</sup> and 15.1μgmL<sup>-1</sup>, respectively). These results indicate that T2 tannase treatment of GTE enhanced its radical-scavenging activity, an increase that was also observed in the reaction using EGCG substrate. Taken together, our results revealed that T2 tannase is more suitable for biotransformation of catechins in GTE than T1 tannase, and T2 treatment provides an enhanced radical-scavenging effect.

Original languageEnglish
Pages (from-to)546-553
Number of pages8
JournalJournal of Bioscience and Bioengineering
Volume118
Issue number5
DOIs
Publication statusPublished - 2014 Nov 1

Fingerprint

tannase
Enzyme inhibition
Tea
Biotransformation
Fungi
Substrates
Scavenging
Catechin
Antioxidants

Keywords

  • Antioxidative activity
  • Biotransformation
  • Substrate inhibition
  • Tannase
  • Tea catechins

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Bioengineering

Cite this

Differential activities of fungi-derived tannases on biotransformation and substrate inhibition in green tea extract. / Baik, Joo Hyun; Suh, Hyung Joo; Cho, So Young; Park, Yooheon; Choi, Hyeon Son.

In: Journal of Bioscience and Bioengineering, Vol. 118, No. 5, 01.11.2014, p. 546-553.

Research output: Contribution to journalArticle

@article{50685d0f6f5d4163b4d938d88e6e5327,
title = "Differential activities of fungi-derived tannases on biotransformation and substrate inhibition in green tea extract",
abstract = "Tannases are important enzymes in the antioxidant potential of tea leaves. In this study, we evaluated the effect of two tannases (T1 and T2) on biotransformation of tea polyphenols and antioxidative activities from catechins in green tea extract (GTE). The T1 tannase-catalyzed reaction was inhibited by the addition of >2.0{\%} GTE substrate, whereas the T2-catalyzed reaction was not inhibited, even by addition of 5.0{\%} GTE. Furthermore, the T1 tannase-catalyzed reaction was inhibited by addition of 10mgmL-1 EGCG, whereas the T2 tannase-catalyzed reaction did not display any inhibitory effect. These results indicate that T2 tannase was more tolerant than T1 tannase to substrate inhibition in degallation reactions. Specifically, the substrate EGCG (90,687.1μgmL-1) was transformed into gallic acid (50,242.9μgmL-1) and EGC (92,598.3μgmL-1) after 1-h treatment with T2 tannase (500Ug-1). The tannase-mediated product displayed higher in vitro radical-scavenging activity than the control. IC50 value of GTE on ABTS and DPPH radicals (46.1μgmL-1 and 18.4μgmL-1, respectively) decreased markedly after T2 tannase treatment (to 35.8μgmL-1 and 15.1μgmL-1, respectively). These results indicate that T2 tannase treatment of GTE enhanced its radical-scavenging activity, an increase that was also observed in the reaction using EGCG substrate. Taken together, our results revealed that T2 tannase is more suitable for biotransformation of catechins in GTE than T1 tannase, and T2 treatment provides an enhanced radical-scavenging effect.",
keywords = "Antioxidative activity, Biotransformation, Substrate inhibition, Tannase, Tea catechins",
author = "Baik, {Joo Hyun} and Suh, {Hyung Joo} and Cho, {So Young} and Yooheon Park and Choi, {Hyeon Son}",
year = "2014",
month = "11",
day = "1",
doi = "10.1016/j.jbiosc.2014.04.012",
language = "English",
volume = "118",
pages = "546--553",
journal = "Journal of Bioscience and Bioengineering",
issn = "1389-1723",
publisher = "Elsevier",
number = "5",

}

TY - JOUR

T1 - Differential activities of fungi-derived tannases on biotransformation and substrate inhibition in green tea extract

AU - Baik, Joo Hyun

AU - Suh, Hyung Joo

AU - Cho, So Young

AU - Park, Yooheon

AU - Choi, Hyeon Son

PY - 2014/11/1

Y1 - 2014/11/1

N2 - Tannases are important enzymes in the antioxidant potential of tea leaves. In this study, we evaluated the effect of two tannases (T1 and T2) on biotransformation of tea polyphenols and antioxidative activities from catechins in green tea extract (GTE). The T1 tannase-catalyzed reaction was inhibited by the addition of >2.0% GTE substrate, whereas the T2-catalyzed reaction was not inhibited, even by addition of 5.0% GTE. Furthermore, the T1 tannase-catalyzed reaction was inhibited by addition of 10mgmL-1 EGCG, whereas the T2 tannase-catalyzed reaction did not display any inhibitory effect. These results indicate that T2 tannase was more tolerant than T1 tannase to substrate inhibition in degallation reactions. Specifically, the substrate EGCG (90,687.1μgmL-1) was transformed into gallic acid (50,242.9μgmL-1) and EGC (92,598.3μgmL-1) after 1-h treatment with T2 tannase (500Ug-1). The tannase-mediated product displayed higher in vitro radical-scavenging activity than the control. IC50 value of GTE on ABTS and DPPH radicals (46.1μgmL-1 and 18.4μgmL-1, respectively) decreased markedly after T2 tannase treatment (to 35.8μgmL-1 and 15.1μgmL-1, respectively). These results indicate that T2 tannase treatment of GTE enhanced its radical-scavenging activity, an increase that was also observed in the reaction using EGCG substrate. Taken together, our results revealed that T2 tannase is more suitable for biotransformation of catechins in GTE than T1 tannase, and T2 treatment provides an enhanced radical-scavenging effect.

AB - Tannases are important enzymes in the antioxidant potential of tea leaves. In this study, we evaluated the effect of two tannases (T1 and T2) on biotransformation of tea polyphenols and antioxidative activities from catechins in green tea extract (GTE). The T1 tannase-catalyzed reaction was inhibited by the addition of >2.0% GTE substrate, whereas the T2-catalyzed reaction was not inhibited, even by addition of 5.0% GTE. Furthermore, the T1 tannase-catalyzed reaction was inhibited by addition of 10mgmL-1 EGCG, whereas the T2 tannase-catalyzed reaction did not display any inhibitory effect. These results indicate that T2 tannase was more tolerant than T1 tannase to substrate inhibition in degallation reactions. Specifically, the substrate EGCG (90,687.1μgmL-1) was transformed into gallic acid (50,242.9μgmL-1) and EGC (92,598.3μgmL-1) after 1-h treatment with T2 tannase (500Ug-1). The tannase-mediated product displayed higher in vitro radical-scavenging activity than the control. IC50 value of GTE on ABTS and DPPH radicals (46.1μgmL-1 and 18.4μgmL-1, respectively) decreased markedly after T2 tannase treatment (to 35.8μgmL-1 and 15.1μgmL-1, respectively). These results indicate that T2 tannase treatment of GTE enhanced its radical-scavenging activity, an increase that was also observed in the reaction using EGCG substrate. Taken together, our results revealed that T2 tannase is more suitable for biotransformation of catechins in GTE than T1 tannase, and T2 treatment provides an enhanced radical-scavenging effect.

KW - Antioxidative activity

KW - Biotransformation

KW - Substrate inhibition

KW - Tannase

KW - Tea catechins

UR - http://www.scopus.com/inward/record.url?scp=84927178280&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84927178280&partnerID=8YFLogxK

U2 - 10.1016/j.jbiosc.2014.04.012

DO - 10.1016/j.jbiosc.2014.04.012

M3 - Article

C2 - 24856576

AN - SCOPUS:84927178280

VL - 118

SP - 546

EP - 553

JO - Journal of Bioscience and Bioengineering

JF - Journal of Bioscience and Bioengineering

SN - 1389-1723

IS - 5

ER -