Purification and partial characterisation of a 1.57 kDa thermostable esterase from Bacillus stearothermophilus

Davina De C.M. Simoes; David McNeill; Bjorn Kristiansen; Michael Mattey

doi:10.1016/S0378-1097(96)00520-4

Purification and partial characterisation of a 1.57 kDa thermostable esterase from Bacillus stearothermophilus

Davina De C.M. Simoes, David McNeill, Bjorn Kristiansen, Michael Mattey

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20 Citations (Scopus)

Abstract

The molecular mass of esterases usually falls in the range of 20-160 kDa, although an esterase of 5.7 kDa from Candida lipolytica has been described. Three other enzymes smaller than 10 kDa have been reported, all of which were more thermostable than their higher molecular mass counterparts. This paper describes the purification of an extracellular esterase hydrolysing fluorescein dibutyrate from Bacillus stearothermophilus NCIMB 13335. The esterase had a molecular mass of 1.57 kDa when analysed by SDS-PAGE, gel filtration and MALDI-TOF spectrometry. This enzyme retained more than 90% of its activity after incubation at 90°C for 2 h.

Original language	English
Pages (from-to)	151-156
Number of pages	6
Journal	FEMS Microbiology Letters
Volume	147
Issue number	1
DOIs	https://doi.org/10.1016/S0378-1097(96)00520-4
Publication status	Published - 1 Feb 1997

Keywords

Bacillus stearothermophilus
esterase
low molecular mass enzyme
thermostability

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10.1016/S0378-1097(96)00520-4

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title = "Purification and partial characterisation of a 1.57 kDa thermostable esterase from Bacillus stearothermophilus",

abstract = "The molecular mass of esterases usually falls in the range of 20-160 kDa, although an esterase of 5.7 kDa from Candida lipolytica has been described. Three other enzymes smaller than 10 kDa have been reported, all of which were more thermostable than their higher molecular mass counterparts. This paper describes the purification of an extracellular esterase hydrolysing fluorescein dibutyrate from Bacillus stearothermophilus NCIMB 13335. The esterase had a molecular mass of 1.57 kDa when analysed by SDS-PAGE, gel filtration and MALDI-TOF spectrometry. This enzyme retained more than 90\% of its activity after incubation at 90°C for 2 h.",

keywords = "Bacillus stearothermophilus, esterase, low molecular mass enzyme, thermostability",

author = "Simoes, \{Davina De C.M.\} and David McNeill and Bjorn Kristiansen and Michael Mattey",

note = "Funding Information: The authors wish to thank The University of Aberdeen Protein Sequence Facility for the MALDI and amino acid analysis. Financial support from the Brazilian National Council of Research and Development (Bolsista do CNPq-Bras{\'ı}lia/Brazil) to D. Simoes is also gratefully acknowledged. ",

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doi = "10.1016/S0378-1097(96)00520-4",

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T1 - Purification and partial characterisation of a 1.57 kDa thermostable esterase from Bacillus stearothermophilus

AU - Simoes, Davina De C.M.

AU - McNeill, David

AU - Kristiansen, Bjorn

AU - Mattey, Michael

N1 - Funding Information: The authors wish to thank The University of Aberdeen Protein Sequence Facility for the MALDI and amino acid analysis. Financial support from the Brazilian National Council of Research and Development (Bolsista do CNPq-Brası́lia/Brazil) to D. Simoes is also gratefully acknowledged.

PY - 1997/2/1

Y1 - 1997/2/1

N2 - The molecular mass of esterases usually falls in the range of 20-160 kDa, although an esterase of 5.7 kDa from Candida lipolytica has been described. Three other enzymes smaller than 10 kDa have been reported, all of which were more thermostable than their higher molecular mass counterparts. This paper describes the purification of an extracellular esterase hydrolysing fluorescein dibutyrate from Bacillus stearothermophilus NCIMB 13335. The esterase had a molecular mass of 1.57 kDa when analysed by SDS-PAGE, gel filtration and MALDI-TOF spectrometry. This enzyme retained more than 90% of its activity after incubation at 90°C for 2 h.

AB - The molecular mass of esterases usually falls in the range of 20-160 kDa, although an esterase of 5.7 kDa from Candida lipolytica has been described. Three other enzymes smaller than 10 kDa have been reported, all of which were more thermostable than their higher molecular mass counterparts. This paper describes the purification of an extracellular esterase hydrolysing fluorescein dibutyrate from Bacillus stearothermophilus NCIMB 13335. The esterase had a molecular mass of 1.57 kDa when analysed by SDS-PAGE, gel filtration and MALDI-TOF spectrometry. This enzyme retained more than 90% of its activity after incubation at 90°C for 2 h.

KW - Bacillus stearothermophilus

KW - esterase

KW - low molecular mass enzyme

KW - thermostability

UR - https://www.scopus.com/pages/publications/0031056577

U2 - 10.1016/S0378-1097(96)00520-4

DO - 10.1016/S0378-1097(96)00520-4

M3 - Article

AN - SCOPUS:0031056577

SN - 0378-1097

VL - 147

SP - 151

EP - 156

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 1

ER -

Purification and partial characterisation of a 1.57 kDa thermostable esterase from Bacillus stearothermophilus

Abstract

Keywords

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