Improving the Stability of Insulin in Solutions Containing Intestinal Proteases in Vitro

نویسندگان

  • Liefeng Zhang
  • Hui Jiang
  • Wenjie Zhu
  • Lin Wu
  • Lingling Song
  • Qiuyan Wu
  • Yong Ren
چکیده

Degradation of insulin was studied in this work. Casein and protamine could obviously suppress degradation of insulin by intestinal enzymes, and could protect insulin from degradation by the mechanism of competition and combination with proteolysis enzyme. What is more, co-incubated with HP-beta-CD-casein or HP-beta-CD-protamine, most insulin was protected from degradation by intestinal enzymes. In addition, it was found that the complexation of insulin with HP-beta-CD was characterized by UV absorption spectra. These results indicated that HP-beta-CD, casein and protamine could offer some positive and useful results, and could protect insulin from degradation during their transit through the intestinal tract.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Formulation of Insulin Containing Niosomes and the Effect of Their Oral Administration on Blood Glucose in Streptozotocin-induced Diabetic rats

Multilamellar vesicles (noisome) of polyoxyethylene alkyl ether surfactants (Brij 52, 72, 76 and 92) were prepared using classic film hydration method. Vesicle formation ability of the surfactants was assessed in presence or absence of cholesterol. All used surfactants formed vesicles in the absence of cholesterol. Recombinant human insulin was used as a model protein drug to investigate encaps...

متن کامل

Study on Activity and Stability of Proteases from Bacillus Sp. Produced by Submerged Fermentation

Objective: Investigations were carried out to isolate bacteria from saline-alkali soils and determined optimized alkaline protease activity and stability produced by a wild strain of bacillus sp. in submerged fermentation (SMF). Methods: Optimum temperature for enzyme activity in the crude extract was 40 ◦C at a pH between 8.0 and 9.0. The studies on pH stability showed that the enzyme...

متن کامل

Studying the Stability of S-Layer Protein of Lactobacillus Acidophilus ATCC 4356 in Simulated Gastrointestinal Fluids Using SDS-PAGE and Circular Dichroism

Crystalline arrays of proteinaceous subunits forming surface layers (S-layers) are now recognized as one of the most common outermost cell envelope components of prokaryotic organisms. The surface layer protein of Lactobacillus acidophilus ATCC4356 is composed of a single species of protein of apparent molecular weight of 43-46 KDa. Considering the Lactobacillus acidophilus ATCC4356 having the ...

متن کامل

Studying the Stability of S-Layer Protein of Lactobacillus Acidophilus ATCC 4356 in Simulated Gastrointestinal Fluids Using SDS-PAGE and Circular Dichroism

Crystalline arrays of proteinaceous subunits forming surface layers (S-layers) are now recognized as one of the most common outermost cell envelope components of prokaryotic organisms. The surface layer protein of Lactobacillus acidophilus ATCC4356 is composed of a single species of protein of apparent molecular weight of 43-46 KDa. Considering the Lactobacillus acidophilus ATCC4356 having the ...

متن کامل

Study on Activity and Stability of Proteases from Bacillus Sp. Produced by Submerged Fermentation

Objective: Investigations were carried out to isolate bacteria from saline-alkali soils and determined optimized alkaline protease activity and stability produced by a wild strain of bacillus sp. in submerged fermentation (SMF). Methods: Optimum temperature for enzyme activity in the crude extract was 40 ◦C at a pH between 8.0 and 9.0. The studies on pH stability showed that the enzyme...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • International Journal of Molecular Sciences

دوره 9  شماره 

صفحات  -

تاریخ انتشار 2008