Isolation and Identification of Aerobic Endospore-Forming Bacteria

Priest, Fergus G.

doi:10.1007/978-1-4899-3502-1_3

Cited by 27 publications

(24 citation statements)

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“…On microscopic examination tangled coils of long chains of bacilli may be found (Burrows, 1973). Priest (1989) reported the amylolytic, proteolytic and lipolytic (deesterification) activity of this organism. It has ability to secrete high levels of protein into the growth medium.…”

Section: Soybean Fermentation and Fermenting Bacillimentioning

confidence: 99%

“…The nitrogen solubility index of Kinema flours is higher than soyflours. B. subtilis is known to produce a number of proteolytic enzymes which hydrolyze protein to smaller peptides and finally ammonia (Priest, 1989). These chemicals are responsible for increase in water-soluble nitrogen and flavour of Kinema Nikkuni et al, 1995).…”

Section: Physico-chemical Propertiesmentioning

confidence: 99%

See 1 more Smart Citation

Bacillus Fermentation of Soybean: A Review

Shrestha

Dahal²,

Ndungutse

2013

J Food Sci Technol Nepal

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Section: Soybean Fermentation and Fermenting Bacillimentioning

confidence: 99%

Section: Physico-chemical Propertiesmentioning

confidence: 99%

Bacillus Fermentation of Soybean: A Review

Shrestha

Dahal²,

Ndungutse

2013

J Food Sci Technol Nepal

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“…The increase in production of microbial lipases requires not only the techniques of molecular biology which contribute to the overexpression of the corresponding genes, but also the understanding of the molecular and biochemical mechanisms that influence the folding and secretion of these enzymes [6,7,8]. Bacillus lipases have attracted much attention because of their biotechnological potential, which has led to the isolation of several lipolytic enzymes of B. subtilis and other species of the genus Bacillus, Geobacillus and Paenibacillus [9].…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterization of a new thermostable lipase from Bacillus pumilus strain

Faouzi

Bergadi

Sayari³

et al. 2015

Turk J Bioch

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Objective: Research and characterization of new thermostable lipases from bacterial strains isolated from tannery waters in the old medina of Fez. Methods: Gene which encodes the 16S ribosomal RNA for a bacterial species was amplified via PCR and sequenced (Bacillus pumilus HF544325). The extracellular lipase from B. pumilus is purified by gel filtration (Sephacryl S-200) and cation exchange chromatography (Mono S sepharose cation exchanger). The N-terminal sequences of purified Bacillus pumilus lipase were determined by automated Edman's degradation, using an Applied Biosystems 470 A protein sequencer equipped with PTH 120A analyser. The activity of lipase was examined within the pH range of 6.0-10.0 and the effect of pH on lipase stability was determined by incubating the lipase fraction in various buffer solutions ranging from 3.0 to 10.0 for 24 h at room temperature. Results:The results showed that Bacillus pumilus is a strain that produce non-inducible lipase. This enzyme has a molecular weight of 27 kDa and presents a maximal activity at pH 8 and 45°C. The 18 N-terminal amino acid residues showed a high degree of homology with other Bacillus lipase sequences. After treatment in 100°C for 5 min, the thermostable enzyme maintains 60% of its activity, which is greater than that those founded in previous works. The enzyme retained 100% of its activity after 30 min incubation at 70°C. Conclusion: This newly isolated lipase is thermostable and it has a significant difference which was observed when the biochemical properties of the Bacillus pumilus lipase were compared to others microbial lipases. The Bacillus pumilus lipase can be considered as a good candidature for industrial and biotechnological applications. Key Words: Bacillus pumilus, lipase, purification, thermostable Conflict of Interest: The authors have no conflict of interest. ÖZETAmaç: Çalışmanın amacı Fez şehrinde bulunan tabakhane sularından izole edilen bakteri suşla-rından, sıcaklığa dayanıklı yeni bir lipaz enzimini saflaştırarak karakterize etmektir. Metod: Bakteri türleri için 16S ribosomal RNA'yı kodlayan gen PCR ile çoğaltılarak sekanslanmıştır (Bacillus pumilus HF544325). Ekstraselüler lipaz jel filtrasyonu (Sefakril S-200) ve katyon değiştirici kromatografi kullanılarak (Mono S Sefaroz katyon değiştirici) B. pumilus'den saflaştırılmıştır. Saflaştırılan Bacillus pumilus lipazının N-terminal dizisi Edman degredasyon yöntemi (Applied Biosystems 470 A protein sekanslama cihazı ile PTH120A analizör) ile saptanmıştır. Lipaz aktivitesi 6.0-10.0 pH aralığında incelenmiş, pH'nın lipaz enziminin dayanık-lılığına olan etkisi lipaz fraksiyonunu pH'sı 3.0 ile 10.0 arasında değişen çeşitli tampon çözel-tilerinde 24 saat oda sıcaklığında inkübe ederek araştırılmıştır. Bulgular: Sonuçlar Bacillus pumilus suşunun indüklenmeyen lipaz enzimini ürettiğini gös-termektedir. Lipaz enzimi 27 kDa molekül ağırlığına sahip olup, en yüksek aktiviteyi pH 8 ve 45°C'de göstermektedir. Amino ucundaki 18 amino asit diğer Bacillus lipaz dizileri ile yüksek oranda ...

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“…Some enzymes isolated from B. subtilis widely used in dairy products by neutral proteases [35]. B. subtilis is also used for production of amino acids [36].…”

Section: Sponge Microbiologymentioning

confidence: 99%