Calcium Alginate: A Support Material for Immobilization of Proteases from Newly Isolated Strain of Bacillus subtilis KIBGE-HAS

نویسندگان

  • Ali Ul Qader
  • Abida Anwar
  • Shah Ali Ul Qader
  • Aliya Raiz
  • Samina Iqbal
  • Abid Azhar
چکیده

Partially purified neutral protease was entrapped in calcium alginate beads and characterized using casein as a substrate. Temperature and pH maxima of the enzyme showed no changes before and after immobilization and remained stable at 50°C and 7.5 respectively. However substrate concentration for maximum enzyme activity of immobilized enzyme was shifted from 0.45% to 0.8%. Reaction time for immobilized enzyme assay was also increased by 5 minutes with reference to soluble enzyme i.e., from 15 to 20 minutes. Enzyme activity was decreased when the concentration of alginate was increased above 2%. Immobilized enzyme retained its activity for longer time and can be reused upto three times. The storage stability of entrapped protease at 4°C was found upto 10 days, while at 30°C the enzyme lost its activity within three days.

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

Addition of Fillers to Sodium Alginate Solution Improves Stability and Immobilization Capacity of the Resulting Calcium Alginate Beads

Background: Although advantages of immobilization of cells through entrapment in calcium alginate gel beads have already been demonstrated, nevertheless, instability of the beads and the mass transfer limitations remain as the major challenges.Objective: The objective of the present study was to increase the stability, porosity (reduce mass transfer limit...

متن کامل

Immobilization of Alkaline Protease produced from Bacillus Licheniformis PTCC1331 on Calcium Alginate (Its effect on enzymatic activity)

Alkaline Protease enzyme produced from Bacillus Licheniformis PTCC1331 in optimum Condition(Temperature 37 ?C, 150 rpm, PH=10), is immobilized in different concentrations of Sodium Alginate using entrapment method, to increase its thermal resistance in detergents, and its activity is measured thereafter. Maximum enzymatic activity of 46 was obtained in 2%w/v Sodium alginate solution. Investiga...

متن کامل

Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix

Maltase from Bacillus licheniformis KIBGE-IB4 was immobilized within calcium alginate beads using entrapment technique. Immobilized maltase showed maximum immobilization yield with 4% sodium alginate and 0.2 M calcium chloride within 90.0 min of curing time. Entrapment increases the enzyme-substrate reaction time and temperature from 5.0 to 10.0 min and 45 °C to 50 °C, respectively as compared ...

متن کامل

Biodegradation of crude oil by immobilized microbial cells in alginate beads produced by electrospraying technique

Background and Objective: Petroleum compounds are major contributors to aquatic environmental pollution. In recent years, biological treatments as environmental-friendly and cost-effective techniques have been used alongside the various physico-chemical methods. Microbial cell immobilization in hydrogel carriers has been the focus of researchers due to various advantages such as ease of microbi...

متن کامل

Protease Production by Bacillus subtilis Immobilized on Different Matrices

Protease production by Bacillus subtilis with free and immobilized cells was examined in this study. Entrapment method of immobilization was used with gelatin, polyacrylamide, calcium alginate and agar matrices and protease production was studied compared to equivalent weight of free cells. Results showed that the gelatin entrapped cells produce 10.8 U/ml; the maximum enzyme titer followed by p...

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:

دوره   شماره 

صفحات  -

تاریخ انتشار 2013