09 اردیبهشت 1403
داريوش صابري

داریوش صابری

مرتبه علمی: دانشیار
نشانی: دانشکده علوم و فناوری نانو و زیستی - گروه شیمی
تحصیلات: دکترای تخصصی / شیمی
تلفن: 07731222424
دانشکده: دانشکده علوم و فناوری نانو و زیستی

مشخصات پژوهش

عنوان Cellulose-gold nanohybrid as an effective support to enhance the catalytic efficiency and stability of α-amylase from Bacillus aquimaris
نوع پژوهش مقالات در نشریات
کلیدواژه‌ها
α-amylase Hybrid nanoparticles Immobilization Stability Reusability
مجله JOURNAL OF MOLECULAR LIQUIDS
شناسه DOI 10.1016/j.molliq.2023.123399
پژوهشگران مژگان رزاقی (نفر اول) ، احمد همایی (نفر دوم) ، روح الله همتی (نفر سوم) ، داریوش صابری (نفر چهارم) ، سودابه کاووسی پور (نفر پنجم)

چکیده

Cellulose nanocrystals/gold nanoparticle hybrids were synthesized under extreme conditions using hydrothermal treatment without utilizing toxic chemicals. The synthesis of the designed nanohybrid and enzyme immobilization process were confirmed by FT-IR, DLS, intrinsic fluorescence, UV–Vis spectroscopy, FESEM, and EDX techniques. The enzyme, in its free form, exhibited maximum activity at a pH of 10 and a temperature of 70 ◦C. However, when the enzyme was immobilized, its optimal temperature increased to 80 ◦C while its optimal pH remained constant. This catalytic platform significantly improved the thermal and chemical stability, along with enzyme stability at significant pH levels. Following a storage period of four weeks, it was observed that immobilized α-amylase retained 67.5 % of its initial activity, while free α-amylase retained only 17 % of its initial activity. The immobilized α-amylase exhibited a catalytic efficiency of 0.488 mM􀀀 1 s􀀀 1, which was found to be twice as high as that of the free form, which had a catalytic efficiency of 0.254 mM􀀀 1 s􀀀 1. The immobilized enzyme retained its initial activity up to 75 % after 11 consecutive uses. On the basis of the obtained results, it appears that the manufactured immobilized enzyme represents an appropriate choice for industrial use under harsh conditions.