Abstract
Tannin acyl hydrolase also referred as tannase is an enzyme with important applications in several science and technology fields. Due to its hydrolytic and synthetic properties, tannase could be used to reduce the negative effects of tannins in beverages, food, feed, and tannery effluents, for the production of gallic acid from tannin-rich materials, the elucidation of tannin structure, and the synthesis of gallic acid esters in nonaqueous media. However, industrial applications of tannase are still very limited due to its high production cost. Thus, there is a growing interest in the production, recovery, and purification of this enzyme. Recently, there have been published a number of papers on the improvement of upstream and downstream processing of the enzyme. These papers dealt with the search for new tannase producing microorganisms, the application of novel fermentation systems, optimization of culture conditions, the production of the enzyme by recombinant microorganism, and the design of efficient protocols for tannase recovery and purification. The present work reviews the state of the art of basic and biotechnological aspects of tannin acyl hydrolase, focusing on the recent advances in the upstream and downstream processing of the enzyme.
Highlights
Tannin acyl hydrolase known as tannase is an enzyme (EC 3.1.1.20) that catalyzes the hydrolysis of ester bonds present in gallotannins, complex tannins, and gallic acid esters [1, 2]
There have been a number of efforts to improve the production, recovery, and purification processes of the enzyme. These efforts include the looking for new tannase sources [5,6,7,8,9,10,11,12], the development of novel fermentation systems [13,14,15], the optimization of culture conditions [16,17,18,19], the production of the enzyme by recombinant microorganism [20,21,22,23,24], and the design of efficient protocols for tannase recovery and purification [25,26,27]
The induction and repression systems have been studied in submerged- (SmF) and solid-state fermentation systems (SSF) [28, 29]; the physicochemical properties of several tannases have been characterized [7, 12, 20, 30,31,32,33,34,35], and there have been a special interest in the description of tannase and tannase gene structure [21, 36,37,38,39,40,41,42,43,44]
Summary
Tannin acyl hydrolase known as tannase is an enzyme (EC 3.1.1.20) that catalyzes the hydrolysis of ester bonds present in gallotannins, complex tannins, and gallic acid esters [1, 2]. There have been a number of efforts to improve the production, recovery, and purification processes of the enzyme. These efforts include the looking for new tannase sources [5,6,7,8,9,10,11,12], the development of novel fermentation systems [13,14,15], the optimization of culture conditions [16,17,18,19], the production of the enzyme by recombinant microorganism [20,21,22,23,24], and the design of efficient protocols for tannase recovery and purification [25,26,27]. The present work reviews the state of the art of basic and biotechnological aspects of tannin acyl hydrolase, focusing on the recent advances in the upstream and downstream processing of the enzyme
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