Catalysis and stability of an alkaline protease from a haloalkaliphilic bacterium under non-aqueous conditions as a function of pH, salt and temperature

Pandey, Sandeep; Rakholiya, Kalpna; Raval, Vikram H.; Singh, Satya P.

doi:10.1016/j.jbiosc.2012.03.003

Cited by 31 publications

(9 citation statements)

References 45 publications

(36 reference statements)

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“…Likewise, the alkaline protease from coastal isolate Oceanobacillus sp. can withstand at 2 M NaCl and registered maximum protease activity [37] . Marine Alkalibacillus protease also recorded higher activity at 1 M and it retained 61% activity at 3.1 M NaCl concentration [36] .…”

Section: Resultsmentioning

confidence: 95%

Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes

Maruthiah

Somanath

Immanuel

et al. 2015

Biotechnology Reports

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Section: Resultsmentioning

confidence: 95%

Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes

Maruthiah

Somanath

Immanuel

et al. 2015

Biotechnology Reports

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“…Meanwhile, the activity at pH 8 and 9 were about 62% and 52% of that at pH 7, respectively. The decrease might be due to the changes in the ionic structure of the enzyme caused by protonation or deprotonation of the charged groups [27]. The residual activity was still high at pH above 7.…”

Section: Effect Of Temperature and Ph On Protease Activitymentioning

confidence: 98%

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

Iqbalsyah

Malahayati

Atikah

et al. 2019

Journal of Taibah University for Science

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The growing industrial demand for stable proteases has driven this study to purify and partially characterize a protease from a bacterial strain isolated from undersea fumaroles. Phylogenetic analysis of the 400bp conserved area of the 16S rRNA gene indicated that the isolate was related to Geobacillus thermoleovorans strain SGAir 0734. Purification by ammonium sulfate precipitation and anion exchange chromatography produced 118-fold purity. The optimum activity (646 U mL −1 ) of the pure enzyme was observed at 60°C, pH 7 and with 5M sodium chloride addition. The enzyme retained 73% of its activity when in 50% n-hexane, while the activity was only 40% of the control when in 50% ethyl acetate. The enzyme was tested for its leather dehairing capability. It only caused a slight dehairing and produced soft leather. The enzyme may be applied in skin rejuvenation, wrinkle-smoothing, and high-quality suede production industries. ARTICLE HISTORY

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“…Toluene, xylene and cyclohexane [27] Halobiforma BNMIITR DMSO [28] Oceanobacillus sp. Isooctane [29]…”

Section: Editorialmentioning

confidence: 99%

Biotransformation Serves as an Alternative Tool to the Chemical Synthesis

Gupta¹

2018

J Pharmacogenomics Pharmacoproteomics

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Catalysis and stability of an alkaline protease from a haloalkaliphilic bacterium under non-aqueous conditions as a function of pH, salt and temperature

Cited by 31 publications

References 45 publications

Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes

Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes

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

Biotransformation Serves as an Alternative Tool to the Chemical Synthesis

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