کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
70989 | 48859 | 2006 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Substrate specificity of membrane-bound alcohol oxidase from the tobacco hornworm moth (Manduca sexta) female pheromone glands
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
کاتالیزور
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
A putative alcohol oxidase (AO) from abdominal tips (ATs) of Manduca sexta virgin females was studied in a biphasic system hexane/aqueous phosphate buffer. The pH optimum closest to neutral range (6.8) and the temperature optimum closest to room temperature (25 ± 3 °C) were measured for the highest AO activity. AOs that are in intact membranes have long lifespans and may oxidize repeatedly. A high selectivity for primary alcohols of benzylic, saturated, and allylic type was observed. Neither the secondary alcohols nor the primary alcohols with bulky alkyl groups on C2-carbon are oxidized. This pronounced substrate specificity can be used for specific oxidation of alcohols in mixtures.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 38, Issue 1, 2 January 2006, Pages 37–42
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 38, Issue 1, 2 January 2006, Pages 37–42
نویسندگان
Anna Luxová, Aleš Svatoš,