Tannase enzyme: The most promising biocatalyst for food processing industries

Kannan Natarajan, Aravindan Rajendran, Viruthagiri Thangavelu

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Tannase (tannin acyl hydrolase, E.C.3.1.1.20) is an extracellular hydrolase enzyme that catalyzes the hydrolysis of aster and depside bonds in hydrolysable tannins or gallic acid esters, liberating glucose and gallic acid (GA). Tannase cleaves the ester linkages between galloyl groups present in various compounds such as epigallocatechin and epigallocatechin gallate that are present in green tea leaves. The enzyme could be obtained from many sources starting from prokaryotes to higher eukaryotes. Vital minutiae such as regulation pathways, catalytic characteristics and other properties remain unrevealed which limits its usage in large scale. This study essentially elicits the information on tannase substrates, mechanism, applications, and the recent trends in the purification of tannase.

Original languageEnglish
Pages (from-to)221-228
Number of pages8
JournalBiosciences Biotechnology Research Asia
Volume5
Issue number1
Publication statusPublished - 01-06-2008

Fingerprint

Food-Processing Industry
tannase
Tannins
Hydrolases
hydrolases
tannins
food industry
Gallic Acid
epigallocatechin
gallic acid
Depsides
Esters
Enzymes
enzymes
esters
Hydrolyzable Tannins
green tea
Tea
prokaryotic cells
Eukaryota

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Agronomy and Crop Science
  • Drug Discovery

Cite this

Natarajan, Kannan ; Rajendran, Aravindan ; Thangavelu, Viruthagiri. / Tannase enzyme : The most promising biocatalyst for food processing industries. In: Biosciences Biotechnology Research Asia. 2008 ; Vol. 5, No. 1. pp. 221-228.
@article{01cc9174a5a1465a972c161f0a120989,
title = "Tannase enzyme: The most promising biocatalyst for food processing industries",
abstract = "Tannase (tannin acyl hydrolase, E.C.3.1.1.20) is an extracellular hydrolase enzyme that catalyzes the hydrolysis of aster and depside bonds in hydrolysable tannins or gallic acid esters, liberating glucose and gallic acid (GA). Tannase cleaves the ester linkages between galloyl groups present in various compounds such as epigallocatechin and epigallocatechin gallate that are present in green tea leaves. The enzyme could be obtained from many sources starting from prokaryotes to higher eukaryotes. Vital minutiae such as regulation pathways, catalytic characteristics and other properties remain unrevealed which limits its usage in large scale. This study essentially elicits the information on tannase substrates, mechanism, applications, and the recent trends in the purification of tannase.",
author = "Kannan Natarajan and Aravindan Rajendran and Viruthagiri Thangavelu",
year = "2008",
month = "6",
day = "1",
language = "English",
volume = "5",
pages = "221--228",
journal = "Biosciences Biotechnology Research Asia",
issn = "0973-1245",
publisher = "Oriental Scientific Publishing Company",
number = "1",

}

Tannase enzyme : The most promising biocatalyst for food processing industries. / Natarajan, Kannan; Rajendran, Aravindan; Thangavelu, Viruthagiri.

In: Biosciences Biotechnology Research Asia, Vol. 5, No. 1, 01.06.2008, p. 221-228.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Tannase enzyme

T2 - The most promising biocatalyst for food processing industries

AU - Natarajan, Kannan

AU - Rajendran, Aravindan

AU - Thangavelu, Viruthagiri

PY - 2008/6/1

Y1 - 2008/6/1

N2 - Tannase (tannin acyl hydrolase, E.C.3.1.1.20) is an extracellular hydrolase enzyme that catalyzes the hydrolysis of aster and depside bonds in hydrolysable tannins or gallic acid esters, liberating glucose and gallic acid (GA). Tannase cleaves the ester linkages between galloyl groups present in various compounds such as epigallocatechin and epigallocatechin gallate that are present in green tea leaves. The enzyme could be obtained from many sources starting from prokaryotes to higher eukaryotes. Vital minutiae such as regulation pathways, catalytic characteristics and other properties remain unrevealed which limits its usage in large scale. This study essentially elicits the information on tannase substrates, mechanism, applications, and the recent trends in the purification of tannase.

AB - Tannase (tannin acyl hydrolase, E.C.3.1.1.20) is an extracellular hydrolase enzyme that catalyzes the hydrolysis of aster and depside bonds in hydrolysable tannins or gallic acid esters, liberating glucose and gallic acid (GA). Tannase cleaves the ester linkages between galloyl groups present in various compounds such as epigallocatechin and epigallocatechin gallate that are present in green tea leaves. The enzyme could be obtained from many sources starting from prokaryotes to higher eukaryotes. Vital minutiae such as regulation pathways, catalytic characteristics and other properties remain unrevealed which limits its usage in large scale. This study essentially elicits the information on tannase substrates, mechanism, applications, and the recent trends in the purification of tannase.

UR - http://www.scopus.com/inward/record.url?scp=51249087569&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=51249087569&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:51249087569

VL - 5

SP - 221

EP - 228

JO - Biosciences Biotechnology Research Asia

JF - Biosciences Biotechnology Research Asia

SN - 0973-1245

IS - 1

ER -