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

Authors
Baik, Joo HyunSuh, Hyung JooCho, So YoungPark, YooheonChoi, Hyeon-Son
Issue Date
Nov-2014
Publisher
SOC BIOSCIENCE BIOENGINEERING JAPAN
Keywords
Tannase; Biotransformation; Tea catechins; Antioxidative activity; Substrate inhibition
Citation
JOURNAL OF BIOSCIENCE AND BIOENGINEERING, v.118, no.5, pp.546 - 553
Indexed
SCIE
SCOPUS
Journal Title
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
Volume
118
Number
5
Start Page
546
End Page
553
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/96885
DOI
10.1016/j.jbiosc.2014.04.012
ISSN
1389-1723
Abstract
Tannases are important enzymes in the antioxidant potential of tea leaves. In this study, we evaluated the effect of two tannases (T1 and 12) 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 10 mg mL(-1) EGCG, whereas the 12 tannase-catalyzed reaction did not display any inhibitory effect. These results indicate that 12 tannase was more tolerant than T1 tannase to substrate inhibition in degallation reactions. Specifically, the substrate EGCG (90,687.1 mu g mL(-1)) was transformed into gallic acid (50,242.9 mu g mL(-1)) and EGC (92,5983 mu g mL(-1)) after 1-h treatment with T2 tannase (500 U g(-1)). The tannase-mediated product displayed higher in vitro radical-scavenging activity than the control. 1050 value of GTE on ABTS and DPPH radicals (46.1 mu g mL(-1) and 18.4 mu g mL(-1), respectively) decreased markedly after 12 tannase treatment (to 35.8 mu g mL(-1) and 15.1 mu g mL(-1), respectively). These results indicate that 12 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 12 tannase is more suitable for biotransformation of catechins in GTE than T1 tannase, and 12 treatment provides an enhanced radical-scavenging effect. (C) 2014, The Society for Biotechnology, Japan. All rights reserved.
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