A Modular Approach for Interlocking Enzymes in Whatman Paper. Issue 32 (9th July 2018)

• Record Type: Journal Article
• Authors: Riccardi, Caterina; McCormick, Shelby; Kasi, Rajeswari; Kumar, Challa
• Is Part Of: Angewandte Chemie international edition. Volume 57:Issue 32(2018)
• Page Start: 10158
• Page End: 10162
• Publication Date: 2018-07-09
• Subjects: biomaterials -- biosensors -- cellulose -- enzyme stability -- laccase; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201805074
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: A potentially universal approach is presented for enzyme attachment to cellulose that significantly enhances enzyme stability while retaining high activity, and involves no chemical functionalization of cellulose. Bovine serum albumin (BSA) was interlocked in cellulose to form a protein‐friendly surface (named BSA‐Paper), while also providing COOH and NH2 groups for subsequent attachment of enzymes. The desired enzyme is then mixed with additional BSA and interlocked on BSA‐Paper. The second BSA layer dilutes and crosslinks the enzyme for improved stability. Laccase was tested as a model enzyme for interlocking on BSA‐Paper, and was found to retain over 100 % activity and was 240 times more stable at 25 °C (half life=180 d) than laccase. This new approach was also tested with a few other enzymes with encouraging results, thus providing a potentially universal method for stabilization of enzymes on cellulose with retention of high activities. Abstract : Interlocking of enzymes with BSA in Whatman filter paper by carbodiimide chemistry. This results in a highly stable and recyclable, active, and washable biomaterial with high enzyme loading that is stable at room temperature.