Purification and Characterization of a Polyextremophilic α-Amylase from an Obligate Halophilic Aspergillus penicillioides Isolate and Its Potential for Souse with Detergents
المؤلفون المشاركون
Ali, Imran
Anwar, Mohammad
Prasongsuk, Sehanat
Lotrakul, Pongtharin
Punnapayak, Hunsa
Akbar, Ali
المصدر
العدد
المجلد 2015، العدد 2015 (31 ديسمبر/كانون الأول 2015)، ص ص. 1-8، 8ص.
الناشر
Hindawi Publishing Corporation
تاريخ النشر
2015-06-09
دولة النشر
مصر
عدد الصفحات
8
التخصصات الرئيسية
الملخص EN
An extracellular α-amylase from the obligate halophilic Aspergillus penicillioides TISTR3639 strain was produced and enriched to apparent homogeneity by ammonium sulfate precipitation and Sephadex G100 gel filtration column chromatography.
The mass of the purified amylase was estimated to be 42 kDa by SDS-PAGE.
With soluble starch as the substrate it had a specific activity of 118.42 U·mg−1 and Vmax and Km values of 1.05 µmol·min−1·mg−1 and 5.41 mg·mL−1, respectively.
The enzyme was found to have certain polyextremophilic characteristics, with an optimum activity at pH 9, 80°C, and 300 g·L−1 NaCl.
The addition of CaCl2 at 2 mM was found to slightly enhance the amylase activity, while ZnCl2, FeCl2, or EDTA at 2 mM was strongly or moderately inhibitory, respectively, suggesting the requirement for a (non-Fe2+ or Zn2+) divalent cation.
The enzyme retained more than 80% of its activity when incubated with three different laundry detergents and had a better performance compared to a commercial amylase and three detergents in the presence of increasing NaCl concentrations up to 300 g·L−1.
Accordingly, it has a good potential for use as an α-amylase in a low water activity (high salt concentration) and at high pH and temperatures.
نمط استشهاد جمعية علماء النفس الأمريكية (APA)
Ali, Imran& Akbar, Ali& Anwar, Mohammad& Prasongsuk, Sehanat& Lotrakul, Pongtharin& Punnapayak, Hunsa. 2015. Purification and Characterization of a Polyextremophilic α-Amylase from an Obligate Halophilic Aspergillus penicillioides Isolate and Its Potential for Souse with Detergents. BioMed Research International،Vol. 2015, no. 2015, pp.1-8.
https://search.emarefa.net/detail/BIM-1054737
نمط استشهاد الجمعية الأمريكية للغات الحديثة (MLA)
Ali, Imran…[et al.]. Purification and Characterization of a Polyextremophilic α-Amylase from an Obligate Halophilic Aspergillus penicillioides Isolate and Its Potential for Souse with Detergents. BioMed Research International No. 2015 (2015), pp.1-8.
https://search.emarefa.net/detail/BIM-1054737
نمط استشهاد الجمعية الطبية الأمريكية (AMA)
Ali, Imran& Akbar, Ali& Anwar, Mohammad& Prasongsuk, Sehanat& Lotrakul, Pongtharin& Punnapayak, Hunsa. Purification and Characterization of a Polyextremophilic α-Amylase from an Obligate Halophilic Aspergillus penicillioides Isolate and Its Potential for Souse with Detergents. BioMed Research International. 2015. Vol. 2015, no. 2015, pp.1-8.
https://search.emarefa.net/detail/BIM-1054737
نوع البيانات
مقالات
لغة النص
الإنجليزية
الملاحظات
Includes bibliographical references
رقم السجل
BIM-1054737
قاعدة معامل التأثير والاستشهادات المرجعية العربي "ارسيف Arcif"
أضخم قاعدة بيانات عربية للاستشهادات المرجعية للمجلات العلمية المحكمة الصادرة في العالم العربي
تقوم هذه الخدمة بالتحقق من التشابه أو الانتحال في الأبحاث والمقالات العلمية والأطروحات الجامعية والكتب والأبحاث باللغة العربية، وتحديد درجة التشابه أو أصالة الأعمال البحثية وحماية ملكيتها الفكرية. تعرف اكثر