Spectrophotometric assay of immobilized tannase

Katwa, Laxmansa C.; Ramakrishna, M.; Rao, M. R. Raghavendra

doi:10.1007/bf02702656

Cited by 33 publications

(18 citation statements)

References 8 publications

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“…Being a natural polymer, collagen has been used for immobilization of tannase employing glutaraldehyde as cross-linking agent (Katwa et al 1981). Fe 3+ -collagen fibers proved to be excellent supporting matrix for catalase immobilization by retaining significant activity even after 26 reuses (Chen et al 2011b).…”

Section: Materials Used For Fabrication Of Immobilization Supportsmentioning

confidence: 99%

“…In cross-linking/covalent method, bi/multifunctional reagents such as glutaraldehyde, bisdiazobenzidine and hexamethylene diisocyanate are used (Lee et al 2006; Singh 2009). Polymers like collagen, cellulose and κ-carrageenan are employed by entrapment method, while the membrane confinement method includes formulation of liposomes and microcapsules (Katwa et al 1981; Wang and Hettwer 1982; Mislovicová et al 2004; Hilal et al 2006; Tümtürk et al 2007; Rochefort et al 2008; Jegannathan et al 2010; Chen et al 2011a, b; Klein et al 2011). …”

Section: Introductionmentioning

confidence: 99%

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Enzyme immobilization: an overview on techniques and support materials

2012

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The current demands of the world’s biotechnological industries are enhancement in enzyme productivity and development of novel techniques for increasing their shelf life. These requirements are inevitable to facilitate large-scale and economic formulation. Enzyme immobilization provides an excellent base for increasing availability of enzyme to the substrate with greater turnover over a considerable period of time. Several natural and synthetic supports have been assessed for their efficiency for enzyme immobilization. Nowadays, immobilized enzymes are preferred over their free counterpart due to their prolonged availability that curtails redundant downstream and purification processes. Future investigations should endeavor at adopting logistic and sensible entrapment techniques along with innovatively modified supports to improve the state of enzyme immobilization and provide new perspectives to the industrial sector.

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Section: Materials Used For Fabrication Of Immobilization Supportsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Enzyme immobilization: an overview on techniques and support materials

2012

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“…For industrial application, the immobilized form of enzyme offers several advantages, including repeated use of the enzyme, ease of product separation, improvement of enzyme stability and continuous operation in packed‐bed reactors. However, there are few reports on immobilized tannases ( Weetal & Dater 1974; Katwa et al . 1981 ; Weetal 1985).…”

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confidence: 99%

Immobilization of Aspergillus oryzae tannase and properties of the immobilized enzyme

et al. 1999

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. Tannase enzyme from Aspergillus oryzae was immobilized on various carriers by different methods. The immobilized enzyme on chitosan with a bifunctional agent (glutaraldehyde) had the highest activity. The catalytic properties and stability of the immobilized tannase were compared with the corresponding free enzyme. The bound enzyme retained 20·3% of the original specific activity exhibited by the free enzyme. The optimum pH of the immobilized enzyme was shifted to a more acidic range compared with the free enzyme. The optimum temperature of the reaction was determined to be 40°C for the free enzyme and 55°C for the immobilized form. The stability at low pH, as well as thermal stability, were significantly improved by the immobilization process. The immobilized enzyme exhibited mass transfer limitation as reflected by a higher apparent K m value and a lower energy of activation. The immobilized enzyme retained about 85% of the initial catalytic activity, even after being used 17 times.

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“…However, there are few reports regarding immobilized tannases from Paecilomyces variotii (Katwa et al, 1981;Weetal, 1985;Mohapatra et al, 2007). One of the most suitable methods for enzyme immobilization is entrapment in alginate because this polysaccharide is a biocompatible and biodegradable material; the technique is simple, nontoxic and cheap.…”

Section: Introductionmentioning

confidence: 99%

Immobilization ofPaecilomyces variotiitannase and properties of the immobilized enzyme

Schons

Lopes

Battestin

et al. 2011

Journal of Microencapsulation

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Tannase produced by Paecilomyces variotii was encapsulated in sodium alginate beads and used for the effective hydrolysis of tannic acid; the efficiency of hydrolysis was comparable to that of the free enzyme. The alginate beads retained 100% of their efficiency in the first three rounds of successive use and 60% in rounds 4 and 5. The response surface methodology showed that the best conditions to hydrolysis of tannic acid by immobilized tannase were: sodium alginate 5.2%, CaCl₂ 0.55 M and 9 h to curing time. The optimized process resulted in 2.4 times more hydrolysed tannic acid than that obtained before optimization. The optimum pH for the actions of both the encapsulated and the free enzymes was 5.5. The optimum temperature of the reaction was determined to be 40 °C for the free enzyme and 60 °C for the immobilized form. The immobilization process improved the stability at low pH.

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Spectrophotometric assay of immobilized tannase

Cited by 33 publications

References 8 publications

Enzyme immobilization: an overview on techniques and support materials

Enzyme immobilization: an overview on techniques and support materials

Immobilization of Aspergillus oryzae tannase and properties of the immobilized enzyme

Immobilization ofPaecilomyces variotiitannase and properties of the immobilized enzyme

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