Preparation and Properties of Enzyme-Immobilized Porous Polypropylene Films

✍ Scribed by Akihiko Tanioka; Yutaka Yokoyama; Keizo Miyasaka

• Publisher: Elsevier Science
• Year: 1998
• Tongue: English
• Weight: 96 KB
• Volume: 200
• Category: Article
• ISSN: 0021-9797
• DOI: 10.1006/jcis.1997.5326

✦ Synopsis

ARTICLE NO. CS975326 NOTE Preparation and Properties of Enzyme-Immobilized Porous Polypropylene Films tion disappeared from it. With the series of procedures previously mentioned, invertase was entrapped in the pores of the membrane. After the The possibility of an enzyme-immobilized membrane using inexternal surfaces of the membrane were cleaned with filter paper, the memvertase-entrapped polyolefin porous films such as porous polyprobrane was dried in a desiccator. The dried sample was placed in the glass pylene films with plasma-induced graft polymerization is disreactor tube, the air pressure was reduced to ca. 10 02 torr with a vacuum cussed. Even though plasma-induced graft polymerization on the pump, and plasma was generated via aluminum electrodes and a plasma membrane surface is a very rough method, we performed it withgenerator (Samco PFG-200) (6). The plasma exposure to the film was out losing the enzyme activity. This simple method will signififollowed by immersion in degassed acrylic acid (Wako Pure Chemical cantly aid in applications for engineering use of enzyme-immobi-Industries, Ltd.). Polymerization proceeded in a water bath of 45ЊC for lized membranes. ᭧ 1998 Academic Press either 5 or 20 min. The monomer was grafted on both surfaces of the porous Key Words: membrane; enzyme immobilization; porous polypropolyolefin at the same time. The membrane that was graft-polymerized for pylene film; plasma-induced graft polymerization; invertase. 20 min is called the ''high''-grafting membrane and the one that was graftpolymerized for 5 min is called the ''low''-grafting membrane. The reaction conditions are shown in Table 1 ( 7). IR spectra of the prepared sample were measured to confirm whether the invertase was entrapped in the membrane pore.