Purification and characterization of an extracellular lipase from a newly isolated thermophilic Bacillus pumilus

Joyce Jose, G. Muraleedhara Kurup

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

An extracellular lipase was isolated and purified from a bacterium and is the first report on the isolation and purification of lipase from the species B. pumilus. Effect of temperature, pH and composition of culture medium were optimized for maximum lipase production. The enzyme was purified and the purity was found to be 98%. The Km value of the enzyme was 1.75 x 10-2 mg. and it was found to be a monomer by SDS PAGE. This lipase was found to be alkaline and thermostable and was not a metalloprotein as evidenced from EDTA treatment. Immobilized whole cells were found to be more stable than the pure enzyme.

Original languageEnglish (US)
Pages (from-to)1213-1217
Number of pages5
JournalIndian Journal of Experimental Biology
Volume37
Issue number12
StatePublished - Dec 1 1999

Fingerprint

Lipase
Enzymes
Metalloproteins
Immobilized Cells
Edetic Acid
Culture Media
Polyacrylamide Gel Electrophoresis
Bacteria
Temperature
Bacillus pumilus

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Molecular Biology
  • Cell Biology

Cite this

@article{2a5d50f2bd49425f9a2ffe4e851e2f8f,
title = "Purification and characterization of an extracellular lipase from a newly isolated thermophilic Bacillus pumilus",
abstract = "An extracellular lipase was isolated and purified from a bacterium and is the first report on the isolation and purification of lipase from the species B. pumilus. Effect of temperature, pH and composition of culture medium were optimized for maximum lipase production. The enzyme was purified and the purity was found to be 98{\%}. The Km value of the enzyme was 1.75 x 10-2 mg. and it was found to be a monomer by SDS PAGE. This lipase was found to be alkaline and thermostable and was not a metalloprotein as evidenced from EDTA treatment. Immobilized whole cells were found to be more stable than the pure enzyme.",
author = "Joyce Jose and {Muraleedhara Kurup}, G.",
year = "1999",
month = "12",
day = "1",
language = "English (US)",
volume = "37",
pages = "1213--1217",
journal = "Journal of scientific & industrial research. C. Biological sciences",
issn = "0019-5189",
publisher = "National Institute of Science Communication",
number = "12",

}

Purification and characterization of an extracellular lipase from a newly isolated thermophilic Bacillus pumilus. / Jose, Joyce; Muraleedhara Kurup, G.

In: Indian Journal of Experimental Biology, Vol. 37, No. 12, 01.12.1999, p. 1213-1217.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Purification and characterization of an extracellular lipase from a newly isolated thermophilic Bacillus pumilus

AU - Jose, Joyce

AU - Muraleedhara Kurup, G.

PY - 1999/12/1

Y1 - 1999/12/1

N2 - An extracellular lipase was isolated and purified from a bacterium and is the first report on the isolation and purification of lipase from the species B. pumilus. Effect of temperature, pH and composition of culture medium were optimized for maximum lipase production. The enzyme was purified and the purity was found to be 98%. The Km value of the enzyme was 1.75 x 10-2 mg. and it was found to be a monomer by SDS PAGE. This lipase was found to be alkaline and thermostable and was not a metalloprotein as evidenced from EDTA treatment. Immobilized whole cells were found to be more stable than the pure enzyme.

AB - An extracellular lipase was isolated and purified from a bacterium and is the first report on the isolation and purification of lipase from the species B. pumilus. Effect of temperature, pH and composition of culture medium were optimized for maximum lipase production. The enzyme was purified and the purity was found to be 98%. The Km value of the enzyme was 1.75 x 10-2 mg. and it was found to be a monomer by SDS PAGE. This lipase was found to be alkaline and thermostable and was not a metalloprotein as evidenced from EDTA treatment. Immobilized whole cells were found to be more stable than the pure enzyme.

UR - http://www.scopus.com/inward/record.url?scp=6744231352&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=6744231352&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:6744231352

VL - 37

SP - 1213

EP - 1217

JO - Journal of scientific & industrial research. C. Biological sciences

JF - Journal of scientific & industrial research. C. Biological sciences

SN - 0019-5189

IS - 12

ER -