Loading...
Search for:
bacillus-licheniformis
0.004 seconds
Some investigations on protease enzyme production kinetics using bacillus licheniformis BBRC 100053 and effects of inhibitors on protease activity
, Article International Journal of Chemical Engineering ; 2014 ; ISSN: 1687806X ; Yaghmaei, S ; Moghadam, N ; Sadeghein, B ; Sharif University of Technology
Abstract
Due to great commercial application of protease, it is necessary to study kinetic characterization of this enzyme in order to improve design of enzymatic reactors. In this study, mathematical modeling of protease enzyme production kinetics which is derived from Bacillus licheniformis BBRC 100053 was studied (at 37°C, pH 10 after 73 h in stationary phase, and 150 rpm). The aim of the present paper was to determine the best kinetic model and kinetic parameters for production of protease and calculating K i (inhibition constant) of different inhibitors to find the most effective one. The kinetic parameters K m (Michaelis-Menten constant) and V m (maximum rate) were calculated 0.626 mM and...
Alkaline protease production by immobilized cells using B. licheniformis
, Article Scientia Iranica ; Volume 20, Issue 3 , 2013 , Pages 607-610 ; 10263098 (ISSN) ; Kazemi, A ; Nahid, P ; Yaghmaei, S ; Sabzevari, M. A ; Sharif University of Technology
2013
Abstract
In recent years there has been potential increase in the use of alkaline protease as industrial catalysts. Many major industrial and commercial applications, such as food and textile industries, and medical diagnoses, are highly dependent on the protease enzyme. In the cell immobilization technique, the free movement of microorganisms is restricted in the process, and a continuous system of fermentation can be used. In the present work, this technique has been used for alkaline protease production using different carriers, such as chitosan, corn cob and corn tassel. Enzyme activity before immobilization (72 h) was 78.3 U/ml. Corn cob, with 65% immobilization capacity and the highest enzyme...
Production of extracellular protease and determination of optimise condition by bacillus licheniformis BBRC 100053
, Article Chemical Engineering Transactions ; Volume 21 , 2010 , Pages 1447-1452 ; 19749791 (ISSN) ; 9788895608051 (ISBN) ; Yaghmaei, S ; Haji Hosseini, R ; Sharif University of Technology
Abstract
The production of protease by Bacillus licheniformis BBRC 100053 was studied. The most appropriate medium for the growth and protease production is composed of: lactose 1 %, yeast extract 0.5 %, peptone 0.5 %, KH 2PO4 0.1%, MgSO4.7H2O 0.02 %. Enzyme production corresponded with growth and reached a maximums level (589 U/ml) during the stationary phase at 35 °C, pH equivalent to 10 and with 150 rpm after 73 hours. Protease activity was highest at pH 8 and 45 °C. The best carbon sources are respectively lactose and maltose and the best nitrogen source is peptone The protease was highly active and stable from pH 7.0 to 11.0 with an optimum at pH 7-8.Thermo stability of the enzyme was considered...
Production of extracellular protease and determination of optimal condition by bacillus licheniformis BBRC 100053
, Article International Journal of Engineering, Transactions B: Applications ; Volume 22, Issue 3 , 2009 , Pages 221-228 ; 1728-144X (ISSN) ; Yaghmaei, S ; Haji Hosseini, R ; Sharif University of Technology
Materials and Energy Research Center
2009
Abstract
The production of protease by Bacillus licheniformis BBRC 100053 was studied. The most appropriate medium for the growth and protease production is composed of: lactose 1%, yeast extract 0.5%, peptone 0.5%, KH2 PO 4 0.1%, MgSO4 .7H2 O 0.02%. Enzyme production corresponded with growth and reached a maximums level (589 U/ml) during the stationary phase at 35°C, pH equivalent to 10 and with 150 rpm after 73 hours. Protease activity was highest at pH 8 and 45°C. The best carbon sources are respectively lactose and maltose and the best nitrogen source is peptone. The protease was highly active and stable from pH 7.0 to 11.0 with an optimum at pH 7-8....
Purification and characterization of a novel biosurfactant produced by Bacillus licheniformis MS3
, Article World Journal of Microbiology and Biotechnology ; Volume 26, Issue 5 , 2010 , Pages 871-878 ; 09593993 (ISSN) ; Maghsoudi, E ; Roostaazad, R ; Dadafarin, H ; Sahebghadam Lotfi, A ; Amoozegar, M. A ; Sharif University of Technology
2010
Abstract
The physical properties and chemical structure of a new biosurfactant (licheniformin) produced by Bacillus licheniformis MS3 were investigated. The purified biosurfactant was identified as a lipopeptide with amino acid sequence of Gly, Ala, Val, Asp, Ser, Gly, Tyr and a lactone linkage between the carboxyl group of Aspargine and hydroxyl group of Tyrosine residue. The fatty acid moiety was attached to N-terminal amino acid residue through an amide bond. The purified licheniformin could lower the surface tension of water from 72 to 38 mN/m at concentrations higher than 15 μg/mL and its relative emulsion volume (EV%) was equal to 36%. It also showed stable surface activity over a wide range of...