Enzyme entrapment within hydrophobic and hydrophilic matrices

✍ Scribed by Brown, Harry Darrow ;Patel, Anil B. ;Chattopadhyay, Swaraj K.

• Book ID: 102294602
• Publisher: John Wiley and Sons
• Year: 1968
• Tongue: English
• Weight: 221 KB
• Volume: 2
• Category: Article
• ISSN: 0021-9304
• DOI: 10.1002/jbm.820020206

✦ Synopsis

ATP-diphosphohydrolase, trypsin, and chymotrypsin have been insolubilixed by lattice-entrapment using hydrophilic polyacrylamide gel and hydrophobic Silastic matrices. The entrapped enzymes were stable and unaffected by washing or wet storage. Thermal inactivation properties of polyacrylamide-entrapped ATP-diphosphohydrolae were different from those of the same enzyme in solution. Several substrates were used for each of the proteolytic enzymes. Esterase activities of both trypsin and chymotrypsin were unaltered by entrapment within Silastic. The entrapment of enzymes and other active proteins is potentially of consequence in continuous-flow substrate conversion systems. Silastic with a surface proteolytic activity derived from an entrapped enzyme is of possible medical utility for implantation elements.