کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10234937 | 44955 | 2016 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Substrate specificities of cutinases on aliphatic-aromatic polyesters and on their model substrates
ترجمه فارسی عنوان
خصوصیات زیربنای کرتینازها در پلی استرهای آلیفاتیک-معطر و بر اساس مدلهای آنها
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موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
چکیده انگلیسی
HPLC/MS identification and quantification of the hydrolysis products terephthalic acid (Ta), benzoic acid (Ba), adipic acid (Ada), mono(4-hydroxybutyl) terephthalate (BTa), mono-(2-hydroxyethyl) terephthalate (ETa), mono-(6-hydroxyhexyl) terephthalate (HTa) and bis(4-hydroxybutyl) terephthalate (BTaB) indicated that these enzymes indeed hydrolyze the tested esters. Shorter terminal chain length acids but longer chain length alcohols in oligomeric model substrates were generally hydrolyzed more efficiently. Thc_Cut1 hydrolyzed aromatic ester bonds more efficiently than HiC resulting in up to 3-fold higher concentrations of the monomeric hydrolysis product Ta. Nevertheless, HiC exhibited a higher overall hydrolytic activity on the tested polyesters, resulting in 2-fold higher concentration of released molecules. Thermogravimetry and differential scanning calorimetry (TG-DSC) of the polymeric model substrates revealed a general trend that a lower difference between melting temperature (Tm) and the temperature at which the enzymatic degradation takes place resulted in higher susceptibility to enzymatic hydrolysis.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: New Biotechnology - Volume 33, Issue 2, 25 March 2016, Pages 295-304
Journal: New Biotechnology - Volume 33, Issue 2, 25 March 2016, Pages 295-304
نویسندگان
Veronika Perz, Klaus Bleymaier, Carsten Sinkel, Ulf Kueper, Melanie Bonnekessel, Doris Ribitsch, Georg M. Guebitz,