EXPLORATION OF A HOT SPRING FOR THERMOSTABLE PROTEASE PRODUCERS

Unkeshwar hot spring of Maharashtra was explored for the isolation of industrially important efficient thermostable protease producers. These isolates were identified based on their morphological characters, microscopic features, enzymatic profile and biochemical characteristics as Bacillus sphaeric...

Full description

Saved in:
Bibliographic Details
Published in:Journal of microbiology, biotechnology and food sciences biotechnology and food sciences, 2017-10, Vol.7 (2), p.101-109
Main Authors: Prabhakarrao Pathak, Anupama, Govindrao Rathod, Mukundraj
Format: Article
Language:English
Subjects:
Bacillus
Biochemical characteristics
Biochemistry
Casein
Catalysis
Cations
Detergents
Divalent cations
Food processing
Food processing industry
Magnesium
Molecular weight
pH effects
Pollutants
Protease
Proteases
Proteolysis
Serine
Serine proteinase
Surfactants
Temperature
Thermal stability
Yeast
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Unkeshwar hot spring of Maharashtra was explored for the isolation of industrially important efficient thermostable protease producers. These isolates were identified based on their morphological characters, microscopic features, enzymatic profile and biochemical characteristics as Bacillus sphaericus APP21, Staphylococcus auricularis APP32, Microbacterium sp. APP41, and Kurthia sp. APP42 from Unkeshwar hot spring. Thermostable protease production was carried out using casein-yeast extract medium at 50 oC. Maximum specific activity of partially purified thermostable protease was recorded from Bacillus sphaericus APP21 (447.75 U/mg). Molecular weight of partially purified proteases from these isolates has been determined in the range of 14-29 KDa. These proteases have showed excellent thermostability in the range of temperature 45 to 65 oC. These proteases were catalytically active in the range of pH 7 to 9 and belonged to the class serine protease. Km and Vmax values were found in the range 5.26-8.34 mg/mL and 446-1380 U/mg respectively. The divalent cations Mg2+ and Mn2+ enhanced the catalytic efficiency of these proteases. These proteases showed excellent catalytic efficiency in presence of selected solvents, surfactants and detergents. These properties make them excellent candidates to use in detergent formulation, food processing, and in many biotechnologically important industries where proteolysis is needed at an elevated range of temperature.
ISSN:1338-5178
1338-5178
DOI:10.15414/jmbfs.2017.7.2.101-109