Purification and partial characterization of a thermo-halostable protease produced by <i>Geobacillus</i> sp. strain PLS A isolated from undersea fumaroles

Iqbalsyah, Teuku M.; Malahayati,; Atikah,; Febriani, .

doi:10.1080/16583655.2019.1650489

Cited by 15 publications

(4 citation statements)

References 35 publications

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“…In line with this, the protease of Geobacillus thermoglucosidasius SKF4 from Sungai Klah Hot Spring Park, Malaysia, optimally worked at 60-65 o C and pH 7-8 [35], whereas protease of Geobacillus sp. strain PLS A from undersea fumaroles in Weh Island, Aceh Province, Indonesia, had maximum activity at 60 o C and pH 7 [36]. Also, the protease of Geobacillus toebii LBT 77 newly isolated from a Tunisian hot spring owned a maximum activity at 95 o C and pH 13 [18], while a protease Geobacillus sp.…”

Section: Biochemical Characterization Of Thermostable Proteasementioning

confidence: 98%

Purification and Biochemical Characterization of a Novel Thermostable Serine Protease from Geobacillus sp. GS53

Baykara

Sürmeli

Şanlı‐Mohamed

2021

Appl Biochem Biotechnol

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Proteases account for approximately 60% of the enzyme market in the world, and they are used in various industrial applications including the detergent industry. In this study, production and characterization of a novel serine protease of thermophilic Geobacillus sp. GS53 from Balçova geothermal region, İzmir, Turkey, were performed. The thermostable protease was purified through ammonium sulfate precipitation and anion-exchange chromatography. The results showed that the protease had 137.8 U mg −1 of specific activity and optimally worked at 55 o C and pH 8. It was also active in a broad pH (4-10) and temperature (25-75 °C) ranges. The protease was highly stable at 85 °C and demonstrated relative stability at pH 4, 7, and 10. Also, the enzyme had high stability against organic solvents and surfactants; enzyme relative activity did not decrease below 81% upon preincubation for 10 min. Ca 2+ , Cu 2+ , and Zn 2+ ions slightly induced protease activity. The protease was highly specific to casein, skim milk, Hammerstein casein, and BSA substrates. These results revealed that the protease might have a potential effect in a variety of industrial fields, especially the detergent industry, because of its high thermostability and stability to surfactants.

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Section: Biochemical Characterization Of Thermostable Proteasementioning

confidence: 98%

Purification and Biochemical Characterization of a Novel Thermostable Serine Protease from Geobacillus sp. GS53

Baykara

Sürmeli

Şanlı‐Mohamed

2021

Appl Biochem Biotechnol

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“…The pure enzyme was found to have optimum activity (646 U ml −1 ) at 60 °C, pH 7 and 5 M NaCl addition. The enzyme was tolerant to 50 % hexane and was found to retain 73 % of its activity at this high concentration of hexane [66]. Various other reports have been published regarding the production and characterization of proteases from Geobacillus , and the search for these enzymes is still in progress.…”

Section: Description Of Parageobacillusmentioning

confidence: 99%

A systematic review of the genera Geobacillus and Parageobacillus: their evolution, current taxonomic status and major applications

Najar

Thakur

2020

Microbiology

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The genus Geobacillus , belonging to the phylum Firmicutes, is one of the most important genera and comprises thermophilic bacteria. The genus Geobacillus was erected with the taxonomic reclassification of various Bacillus species. Taxonomic studies of Geobacillus remain in progress. However, there is no comprehensive review of the characteristic features, taxonomic status and study of various applications of this interesting genus. The main aim of this review is to give a comprehensive account of the genus Geobacillus . At present the genus acomprises 25 taxa, 14 validly published (with correct name), nine validly published (with synonyms) and two not validly published species. We describe only validly published species of the genera Geobacillus and Parageobacillus . Vegetative cells of Geobacillus species are Gram-strain-positive or -variable, rod-shaped, motile, endospore-forming, aerobic or facultatively anaerobic, obligately thermophilic and chemo-organotrophic. Growth occurs in the pH range 6.08.5 and a temperature of 37–75 °C. The major cellular fatty acids are iso-C15:o, iso-C16:0 and iso-C17:o. The main menaquinone type is MK-7. The G+C content of the DNA ranges between 48.2 and 58 mol%. The genus Geobacillus is widely distributed in nature, being mostly found in many extreme locations such as hot springs, hydrothermal vents, marine trenches, hay composts, etc. Geobacillus species have been widely exploited in various industrial and biotechnological applications, and thus are promising candidates for further studies in the future.

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“…Microorganisms are found in almost every natural habitat (air, soil, and water), with soil being the most preferred habitat mainly because it serves as a reservoir for diverse microorganisms [ 1 ]. Likewise, protease producing microorganisms are also found everywhere as they have been reported to be isolated from soil [ 2 ], wastewater and sludge [ 3 ], as well as undersea fumaroles [ 4 ]. In fact, some microorganisms can live in areas which are often hostile for the continuation of life having extreme physico-chemical conditions as in alkaline and saline lakes, hot and cold deserts, hot springs and ocean beds.…”

Section: Introductionmentioning

confidence: 99%

Molecular and functional characterization of protease from psychrotrophic Bacillus sp. HM49 in North-western Himalaya

et al. 2023

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In this work, a psychrotrophic bacteria producing cold-active protease, was obtained from Dachigam National Park, an ecologically significant habitat in Western Himalayas owing to its varied endemic and endangered flora and fauna. This isolate was identified as Bacillus sp. HM49 via phenotypic, Gram staining, bio-chemical and 16S rRNA gene identification. Isolate HM49 when tested for proteolytic activity revealed prominent hydrolytic zone with the most production at 20 °C and pH, 8.0 post 72 h incubation. This enzyme was purified, enhancing its specific activity to 61.15 U/mg and its characterization studies revealed it to be a cold-alkaline protease being active in a wide pH (6.0–12) and temperature (5–40 °C) range. Amplification of CAASPR gene of HM49 was performed, followed by enzyme-substrate docking studies and MMGBSA providing details about its type, molecular weight validation as well as functional applications. The purified protease of HM49 was tested for laundry applications and the enzyme was found to be compatible with majority of the detergents tested. Its potential as an eco-friendly detergent additive was further validated by wash performance test as it effectively removed recalcitrant blood stains at a low temperature of 20 °C that could be beneficial for fine garments like silk which preferably need cold washing.

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Purification and partial characterization of a thermo-halostable protease produced by Geobacillus sp. strain PLS A isolated from undersea fumaroles

Cited by 15 publications

References 35 publications

Purification and Biochemical Characterization of a Novel Thermostable Serine Protease from Geobacillus sp. GS53

Purification and Biochemical Characterization of a Novel Thermostable Serine Protease from Geobacillus sp. GS53

A systematic review of the genera Geobacillus and Parageobacillus: their evolution, current taxonomic status and major applications

Molecular and functional characterization of protease from psychrotrophic Bacillus sp. HM49 in North-western Himalaya

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