Bacillus licheniformis BT5.9 isolated from Changar Hot Spring, Malang, Indonesia, as a potential producer of thermostable α-amylase

Darah Ibrahim; Han Li Zhu; Nuraqilah Yusof; Lim Sheh Hong

Bacillus licheniformis BT5.9 isolated from Changar Hot Spring, Malang, Indonesia, as a potential producer of thermostable α-amylase

Darah Ibrahim, Han Li Zhu, Nuraqilah Yusof, Isnaeni, Lim Sheh Hong

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

17 Citations (Scopus)

Abstract

A total of 34 bacterial isolates were obtained from soil samples collected from Changar Hot Spring, Malang, Indonesia. Of these, 13 isolates produced a zone of hydrolysis in starch-nutrient agar medium and generated various amylases in liquid medium. One isolate was selected as the best amylase producer and was identified as Bacillus licheniformis BT5.9. The improvement of culture conditions (initial medium pH of 5.0, cultivation temperature of 50°C, agitation speed of 100 rpm and inoculum size of 1.7 × 10⁹ cells/ml) provided the highest amylase production (0.327 U/ml).

Original language	English
Pages (from-to)	71-84
Number of pages	14
Journal	Tropical Life Sciences Research
Volume	24
Issue number	1
Publication status	Published - Aug 2013
Externally published	Yes

Keywords

Amylase
Bacillus licheniformis
Hot spring
Thermophilic bacteria

Cite this

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title = "Bacillus licheniformis BT5.9 isolated from Changar Hot Spring, Malang, Indonesia, as a potential producer of thermostable α-amylase",

abstract = "A total of 34 bacterial isolates were obtained from soil samples collected from Changar Hot Spring, Malang, Indonesia. Of these, 13 isolates produced a zone of hydrolysis in starch-nutrient agar medium and generated various amylases in liquid medium. One isolate was selected as the best amylase producer and was identified as Bacillus licheniformis BT5.9. The improvement of culture conditions (initial medium pH of 5.0, cultivation temperature of 50°C, agitation speed of 100 rpm and inoculum size of 1.7 × 109 cells/ml) provided the highest amylase production (0.327 U/ml).",

keywords = "Amylase, Bacillus licheniformis, Hot spring, Thermophilic bacteria",

author = "Darah Ibrahim and {Li Zhu}, Han and Nuraqilah Yusof and Isnaeni and {Sheh Hong}, Lim",

year = "2013",

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journal = "Tropical Life Sciences Research",

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T1 - Bacillus licheniformis BT5.9 isolated from Changar Hot Spring, Malang, Indonesia, as a potential producer of thermostable α-amylase

AU - Ibrahim, Darah

AU - Li Zhu, Han

AU - Yusof, Nuraqilah

AU - Isnaeni,

AU - Sheh Hong, Lim

PY - 2013/8

Y1 - 2013/8

N2 - A total of 34 bacterial isolates were obtained from soil samples collected from Changar Hot Spring, Malang, Indonesia. Of these, 13 isolates produced a zone of hydrolysis in starch-nutrient agar medium and generated various amylases in liquid medium. One isolate was selected as the best amylase producer and was identified as Bacillus licheniformis BT5.9. The improvement of culture conditions (initial medium pH of 5.0, cultivation temperature of 50°C, agitation speed of 100 rpm and inoculum size of 1.7 × 109 cells/ml) provided the highest amylase production (0.327 U/ml).

AB - A total of 34 bacterial isolates were obtained from soil samples collected from Changar Hot Spring, Malang, Indonesia. Of these, 13 isolates produced a zone of hydrolysis in starch-nutrient agar medium and generated various amylases in liquid medium. One isolate was selected as the best amylase producer and was identified as Bacillus licheniformis BT5.9. The improvement of culture conditions (initial medium pH of 5.0, cultivation temperature of 50°C, agitation speed of 100 rpm and inoculum size of 1.7 × 109 cells/ml) provided the highest amylase production (0.327 U/ml).

KW - Amylase

KW - Bacillus licheniformis

KW - Hot spring

KW - Thermophilic bacteria

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SN - 1985-3718

VL - 24

SP - 71

EP - 84

JO - Tropical Life Sciences Research

JF - Tropical Life Sciences Research

IS - 1

ER -

Bacillus licheniformis BT5.9 isolated from Changar Hot Spring, Malang, Indonesia, as a potential producer of thermostable α-amylase

Abstract

Keywords

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