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Valorization of Waste and By-products from the agrofood Industry using Fermentation processes and enzyme treatments
Published in Quan V. Vuong, Utilisation of Bioactive Compounds from Agricultural and Food Waste, 2017
Phuong Nguyen Nhat Minh, Thien Trung Le, John Van Camp, Katleen Raes
The enzyme tannin acyl hydrolase, commonly referred to as tannase (EC.3.1.1.20) is involved in biodegradation of tannins into gallic acid and glucose (Chávez-González et al. 2012). There are many studies on the production of tannase using fungi or bacterial species and agro-residues as a substrate. An interesting study was carried out by Lima et al. (2014) in which evaluation of the production of tannase by Aspergillus and Penicillium species through SSF, using leaves and agro-industrial waste, barbados cherry and mangaba fruit, as substrate was obtained. From this study, P. montanense was selected as the best producer of tannase with the highest activity of 42 U/mL (one unit of tannase activity (U) was defined as the amount of enzyme required to release one μmole of gallic acid/min/mL under assay conditions, and was expressed as U/ mL) after 72 hours of fermentation residue, using barbados cherry with 3.5 per cent tannic acid and 70 per cent moisture. The tannase of P. montanense was stable over a wide pH range and temperatures and showed the highest activity at pH 9.0 and 50°C. A recent study demonstrated the benefits of producing tannase (from a low-cost process) for the food industry (Madeira et al. 2015). In this study, citrus residue as a substrate and the fungus strain of Paecilomyces variotii were used for the production of tannase by SSF. The tannase produced showed optimum activity at pH 5.0, with 70°C and 80 per cent stability between pH 4.0–6.5 and 20–60°C. The enzyme was then applied to orange juice and the results showed that tannase on orange juice decreased the levels of hesperidin, naringin and increased their aglycon form, hesperetin and naringenin.
Properties and Applications of the Phytochemical
Published in Cristobal N. Aguilar, Suresh C. Ameta, A. K. Haghi, Green Chemistry and Biodiversity, 2019
René Díaz-Herrera, Pedro Aguilar-Zarate, Juan Alberto Ascasio-Valdes, Leonardo Sepúlveda-Torre, Juan Buenrostro-Figueroa, Monica L. Chavez-Gonzalez, Janeth Ventura, Cristóbal N. Aguilar
Tanin-acyl hydrolase (tannase) is an enzyme that catalyzes the breakdown of hydrolyzable tannins or gallic acid esters. This enzyme can be produced in the presence of tannic acid by some micro-organisms, such as bacteria, yeast, and fungi, the latter being the largest producers of this enzyme. Tannase is used by different industrial sectors such as food, beverages, brewer, pharmaceutical, and chemical.36 The search for new types of tannases with different properties that are as useful for industries and have new applications has been a frequent work since this enzyme was discovered more than 100 years ago.37
Tannin biodegradation by tannase from Serratia marcescens: optimization of production by response surface methodology and its partial characterization
Published in Chemical Engineering Communications, 2021
Amanda Reges de Sena, Lúzia Morgana de Melo Lopes, Miquéas Jamesse Gouveia, Marcos Juliano Gouveia, Marcelo Rodrigues Figueira de Mello, Tonny Cley Campos Leite, Gláucia Manoella de Souza Lima, Keila Aparecida Moreira, Sandra Aparecida de Assis
Tannase (EC: 3.1.1.20) is an enzyme that catalyzes the hydrolysis of tannins into gallic acid and glucose (Deschamps et al. 1983; Jana et al. 2012). It is a membrane-bound or extracellular enzyme produced in the presence of tannic acid, and it can be obtained from vegetable, animal and microbial sources, especially filamentous fungi such as those from genera Aspergillus and Penicillium (Aguilar et al. 1999). However, several researchers have studied the potential of the bacteria to produce extracellular tannase. Some species, such as Bacillus pumilis, Bacillus polymyxa enter the species name in full Klebisiela pneumoniae, Streptococcus bovis and Selenomonas ruminantium, Serratia ficaria, have been used in enzyme production (Belmares et al. 2004; Pepi et al. 2009).
Kinetic, thermodynamic parameters and in vitro digestion of tannase from Aspergillus tamarii URM 7115
Published in Chemical Engineering Communications, 2018
Amanda Reges de Sena, Tonny Cley Campos Leite, Talita Camila Evaristo da Silva Nascimento, Anna Carolina da Silva, Catiane S. Souza, Antônio Fernando de Mello Vaz, Keila Aparecida Moreira, Sandra Aparecida de Assis
Tannase (tannin acyl hydrolase; EC 3.1.1.20) is an enzyme that catalyzes the breakdown of ester and depside bonds of hydrolysable tannins, releasing glucose and gallic acid. It is an inducible extracellular microbial enzyme produced by filamentous fungi, bacteria, and yeasts. The enzyme has been widely applied to the food, pharmaceutical, and chemical industries (Pinto et al., 2006). Among its applications, it is possible mentioning the preparation of instant tea (Lekha and Lonsane, 1997), the manufacturing of beverages such as juices, beer, and wine (Battestin and Macedo, 2007), the propyl-gallate synthesis (Riul et al., 2013), ellagic and gallic acid production (Costa et al., 2013; Robledo et al., 2008), the synthesis of esters and effluent treatment (Mahendran et al., 2006), and additive for feed industry (Nuero and Reyes, 2002).
Co-production of tannase and gallic acid by a novel Penicillium rolfsii (CCMB 714)
Published in Preparative Biochemistry and Biotechnology, 2018
Priscilla Macedo Lima Andrade, Luciana Baptista, Julyana Stoffel Britto, Ana Paula Trovatti Uetenabaro, Andréa Miura da Costa
The main factor for the expression of tannase activity is the carbon source, since most tannases are induced enzymes and are therefore generally produced in the presence of inducers such as tannic acid.[6] In this study, the tannic acid (9.43 U mL−1) and gallic acid (10.40 U mL−1) were the best sources (p<.05) for tannase production when compared to methyl gallate and glucose (Figure 2). Similar results were reported by Costa et al.[20] in studies with Aspergillus tamarii in submerged fermentation, where they obtained tannic activities of 13.1 U mL−1 when the organism was grown in gallic acid, and 9.3 U mL−1 with the use of tannic acid, whereas among the carbon sources tested the highest tannase activity was observed with gallic acid, methyl gallate, and tannic acid. De Melo et al.[21] analyzing the production of tannase in submerged fermentation, also verified that Aspergillus sp. GM4 produced tannase using gallic acid as the only source of carbon in the medium. In this same study, it was observed that 2% tannic acid, 1% methyl gallate, and 1% gallic acid promoted the highest activity of the enzyme, respectively. Corroborating our study, Gonçalves et al. [22] also observed basal levels of tannase production by Aspergillus ochraceus, when the fungus was cultivated only in the presence of glucose.