کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
16942 42625 2015 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Stability and structural changes of horseradish peroxidase: Microwave versus conventional heating treatment
ترجمه فارسی عنوان
پایداری و تغییرات ساختاری پراکسیداز هوررادیش: مایکروویو نسبت به حرارت معمولی
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
چکیده انگلیسی


• HRP activation in CH was related to changes in secondary and tertiary structures.
• HRP treated in MW at 60 °C did not recover the original activity.
• The HRP inactivation in MW was related to loss in the enzyme tertiary structure.

Effects of conventional heating (CH) and microwave (MW) on the structure and activity of horseradish peroxidase (HRP) in buffer solution were studied. CH incubation between 30 and 45 °C increased activity of HRP, reaching 170% of residual activity (RA) after 4–6 h at 45 °C. CH treatment at 50 and 60 °C caused HRP inactivation: RA was 5.7 and 16.7% after 12 h, respectively. Secondary and tertiary HRP structural changes were analyzed by circular dichroism (CD) and intrinsic fluorescence emission, respectively. Under CH, activation of the enzyme was attributed to conformational changes in secondary and tertiary structures. MW treatment had significant effects on the residual activity of HRP. MW treatment at 45 °C/30 W followed by CH treatment 45 °C regenerated the enzyme activity. The greatest loss in activity occurred at 60 °C/60 W/30 min (RA 16.9%); without recovery of the original activity. The inactivation of MW-treated HRP was related to the loss of tertiary structure, indicating changes around the tryptophan environment.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Enzyme and Microbial Technology - Volume 69, February 2015, Pages 10–18
نویسندگان
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