Catalytic properties of lignin peroxidase ALiP-P3 hosted in reversed micelles

✍ Scribed by Junji Michizoe; Shin-ya Okazaki; Masahiro Goto; Shintaro Furusaki

• Book ID: 104419651
• Publisher: Elsevier Science
• Year: 2001
• Tongue: English
• Weight: 110 KB
• Volume: 8
• Category: Article
• ISSN: 1369-703X
• DOI: 10.1016/s1369-703x(01)00093-6

✦ Synopsis

Lignin peroxidase ALiP-P3 from Actinomyces Streptomyces viridosporus T7A (ATCC 39115) became catalytically active by being entrapped in reversed micelles (RM) in an organic solvent. Streptomyces viridosporus T7A was cultivated and the culture supernatant was purified by precipitation with ammonium sulfate and finally ALiP-P3 was concentrated by ultrafiltration. Catalytic performance of lyophilized ALiP-P3 and immobilized ALiP-P3 in RM formulated with a surfactant sodium bis(2-ethylhexyl)sulphosuccinate (AOT) or n-hexadecyl trimethylammonium bromide (CTAB) was investigated by an oxidative reaction. The enzymatic activity was observed only when the enzyme was immobilized in the AOT RM. To optimize the preparation and reaction conditions for ALiP-P3 entrapped in RM, we examined the effects of pH in the water pools of RM, the degree of hydration of the surfactant (Wo), the reaction temperature and the concentration of H 2 O 2 in the reaction medium. ALiP-P3 hosted in RM provided the highest enzymatic activity under the following conditions: pH 9.0, Wo = 20, [H 2 O 2 ] = 40 mM, and 20 • C. The reaction product produced by ALiP-P3 in isooctane was confirmed to be identical to that in aqueous media.