Purification and characterization of a new peptide antibiotic produced by a thermotolerant Bacillus licheniformis strain

Sónia Mendo; Nuno André Faustino; Ana Cristina Sarmento; Francisco Amado; Arthur J.G. Moir

doi:10.1023/B:BILE.0000012888.72489.3f

Purification and characterization of a new peptide antibiotic produced by a thermotolerant Bacillus licheniformis strain

Sónia Mendo^*, Nuno André Faustino, Ana Cristina Sarmento, Francisco Amado, Arthur J.G. Moir

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

42 Citations (Scopus)

Abstract

A Bacillus licheniformis strain, 189, isolated from a hot spring environment in the Azores, Portugal, strongly inhibited growth of Gram-positive bacteria. It produced a peptide antibiotic at 50°C. The antibiotic was purified and biochemically characterized. It was highly resistant to several proteolytic enzymes. Additionally, it retained its antimicrobial activity after incubation at pH values between 3.5 and 8; it was thermostable, retaining about 85% and 20% of its activity after 6 h at 50°C and 100°C, respectively. Its molecular mass determined by mass spectrometry was 3249.7 Da.

Original language	English
Pages (from-to)	115-119
Number of pages	5
Journal	Biotechnology Letters
Volume	26
Issue number	2
DOIs	https://doi.org/10.1023/B:BILE.0000012888.72489.3f
Publication status	Published - Jan 2004
Externally published	Yes

Keywords

Peptide antibiotics
Peptide synthetases
Thermotolerant Bacillus

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10.1023/B:BILE.0000012888.72489.3f

Cite this

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title = "Purification and characterization of a new peptide antibiotic produced by a thermotolerant Bacillus licheniformis strain",

abstract = "A Bacillus licheniformis strain, 189, isolated from a hot spring environment in the Azores, Portugal, strongly inhibited growth of Gram-positive bacteria. It produced a peptide antibiotic at 50°C. The antibiotic was purified and biochemically characterized. It was highly resistant to several proteolytic enzymes. Additionally, it retained its antimicrobial activity after incubation at pH values between 3.5 and 8; it was thermostable, retaining about 85% and 20% of its activity after 6 h at 50°C and 100°C, respectively. Its molecular mass determined by mass spectrometry was 3249.7 Da.",

keywords = "Peptide antibiotics, Peptide synthetases, Thermotolerant Bacillus",

author = "S{\'o}nia Mendo and Faustino, {Nuno Andr{\'e}} and Sarmento, {Ana Cristina} and Francisco Amado and Moir, {Arthur J.G.}",

note = "Funding Information: A.C. Sarmento and N.A. Faustino were supported by Funda{\c c}{\~a}o para a Ci{\^e}ncia e Tecnologia (grants BPD-7183/2001 and BM-20979/1999). Copyright: Copyright 2008 Elsevier B.V., All rights reserved.",

year = "2004",

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doi = "10.1023/B:BILE.0000012888.72489.3f",

language = "English",

volume = "26",

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journal = "Biotechnology Letters",

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AU - Mendo, Sónia

AU - Faustino, Nuno André

AU - Sarmento, Ana Cristina

AU - Amado, Francisco

AU - Moir, Arthur J.G.

N1 - Funding Information: A.C. Sarmento and N.A. Faustino were supported by Fundação para a Ciência e Tecnologia (grants BPD-7183/2001 and BM-20979/1999). Copyright: Copyright 2008 Elsevier B.V., All rights reserved.

PY - 2004/1

Y1 - 2004/1

N2 - A Bacillus licheniformis strain, 189, isolated from a hot spring environment in the Azores, Portugal, strongly inhibited growth of Gram-positive bacteria. It produced a peptide antibiotic at 50°C. The antibiotic was purified and biochemically characterized. It was highly resistant to several proteolytic enzymes. Additionally, it retained its antimicrobial activity after incubation at pH values between 3.5 and 8; it was thermostable, retaining about 85% and 20% of its activity after 6 h at 50°C and 100°C, respectively. Its molecular mass determined by mass spectrometry was 3249.7 Da.

AB - A Bacillus licheniformis strain, 189, isolated from a hot spring environment in the Azores, Portugal, strongly inhibited growth of Gram-positive bacteria. It produced a peptide antibiotic at 50°C. The antibiotic was purified and biochemically characterized. It was highly resistant to several proteolytic enzymes. Additionally, it retained its antimicrobial activity after incubation at pH values between 3.5 and 8; it was thermostable, retaining about 85% and 20% of its activity after 6 h at 50°C and 100°C, respectively. Its molecular mass determined by mass spectrometry was 3249.7 Da.

KW - Peptide antibiotics

KW - Peptide synthetases

KW - Thermotolerant Bacillus

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JF - Biotechnology Letters

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ER -

Purification and characterization of a new peptide antibiotic produced by a thermotolerant Bacillus licheniformis strain

Abstract

Keywords

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