Isolation and characterization of a broad pH- and temperature-active, solvent and surfactant stable protease from a new strain of Bacillus subtilis

Uttatree, Sasithorn; Charoenpanich, Jittima

doi:10.1016/j.bcab.2016.08.003

Cited by 21 publications

(4 citation statements)

References 32 publications

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“…These results, together with the molecular mass obtained, and to the absence of enzymatic inhibition upon the treatment with inhibitors TPCK (irreversible inhibitor of chymotrypsin), pepstatin A (inhibitor of aspartyl protease), E‐64 (irreversible inhibitor of cysteine proteases), and EDTA (chelating Ca 2+ and other divalent metal and acts on metalloproteases and proteases activated by metals), suggest that the enzymes evaluated in this study are trypsins. The weak impact of EDTA on the activity of these enzymes also suggests that such proteases do not rely on any divalent cation, consistent with the fact that proteases are generally independent of cofactors (Uttatree & Charoenpanich, ).…”

Section: Discussionsupporting

confidence: 62%

Purification and characterization of trypsin produced by gut bacteria from Anticarsia gemmatalis

Pilon

Silva

Visôtto

et al. 2017

Arch Insect Biochem Physiol

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Purification of active trypsin in the digestive process of insects is essential for the development of potent protease inhibitors (PIs) as an emerging pest control technology and research into insect adaptations to dietary PIs. An important aspect is the presence of proteolytic microorganisms, which contribute to host nutrition. Here, we purified trypsins produced by bacteria Bacillus cereus, Enterococcus mundtii, Enterococcus gallinarum, and Staphylococcus xylosus isolated from the midgut of Anticarsia gemmatalis. The trypsins had a molecular mass of approximately 25 kDa. The enzymes showed increased activity at 40°C, and they were active at pH values 7.5-10. Aprotinin, bis-benzamidine, and soybean Kunitz inhibitor (SKTI) significantly inhibited trypsin activity. The l-1-tosyl-amido-2-phenylethylchloromethyl ketone (TPCK), pepstatin A, E-64, ethylenediamine tetraacetic acid, and calcium ions did not affect the enzyme activity at the concentrations tested. We infer the purified trypsins do not require calcium ions, by which they differ from the trypsins of other microorganisms and the soluble and insoluble trypsins characterized from A. gemmatalis. These data suggest the existence of different isoforms of trypsin in the velvetbean caterpillar midguts.

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Section: Discussionsupporting

confidence: 62%

Purification and characterization of trypsin produced by gut bacteria from Anticarsia gemmatalis

Pilon

Silva

Visôtto

et al. 2017

Arch Insect Biochem Physiol

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“…thuringiensis MB-3and B. licheniformis AP-2 were the most pH-stable, showing higher hydrolytic activity in all the pH values evaluated (2-12), a feature that deserves to be highlighted due to its industrial interest. Similar characteristic was found for a protease produced by Bacillus sp., which was highly active in a pH range of 3-12, maintaining at least 80 % of its activity, being such a characteristic considered ideal for biotechnological applications (Uttatree and Charoenpanich, 2016).…”

Section: Discussionmentioning

confidence: 99%

Production of thermostable multiple enzymes from Bacillus amyloliquefaciens KUB29

Devaraj

Aathika

Periyasamy

et al. 2018

Natural Product Research

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A strain of Bacillus amyloliquefaciens KUB29 was identified by 16S ribosomal RNA sequencing (Genbank: MF772779.1). Production of thermostable protease, amylase and lipase were done by the isolated strain. The produced enzymes were partially purified by ammonium precipitation followed by dialysis process. Protease and lipase enzymes are effectively used in bio-oil extraction from proteinaceous sample followed by transesterification to produce methyl ester. Amylase enzyme is widely used in food and laundry industry. The produced enzymes are active at thermophilic condition of 55 °C. Use of these enzymes in biofuel production process will make the process cleaner and greener.

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“…Bacterial enzymes are attractive for different reasons such as their enzymes are extracellular and regarded as safe for use. Some of the Bacillus species producing industrially important proteases are Bacillus subtilis and Bacillus licheniformis (Parrado 2014;Uttatree and Charoenpanich 2016).…”

Section: Introductionmentioning

confidence: 99%

Purification, characterization and application of thermoalkaliphilic proteases from Bacillus filamentosus, Lysinibacillus cresolivorans, and Bacillus subtilis

Ullah¹,

Ali²,

Ullah³

et al. 2021

Preprint

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Thermophilic proteases are important industrial enzymes because they can be used at unavoidable temperature in various bioprocessing schemes. The bacterial population of Cholistan desert was explored for thermophillic proteases and their industrial applications. Three bacterial isolates K1, K5, and K7 were found promising protease producers. These isolates were preliminary identified as Bacillus based on morphological characteristics and biochemical tests (positive for catalase, oxidase, and citrate tests, and negative for indole and urease tests). The isolates K1, K5, and K7 were further identified as Bacillus filamentosus, Lysinibacillus cresolivorans, and Bacillus subtilis, respectively by phylogenetic analysis. The isolates grew best at 50oC while Bacillus filamentosus (K1), Lysinibacillus cresolivorans (K5), and Bacillus subtilis (K7) produced larger zones of hydrolysis at 37oC, 45oC and 50oC at pH 7, respectively. The optimum temperature for protease activity was 65oC for Bacillus filamentosus and Lysinibacillus cresolivorans and 55oC for Bacillus subtilis, and the optimum pH for activity was 9 for all the three strains. The protease produced by these isolates were found active at high temperature (37oC to 85oC) and high pH (5–12) which make them industrially important thermoalkaliphilic proteases. Theses proteases successfully de-haired cow’s skin and de-stained blood from cotton cloth pieces, which are rarely tested applications of these proteases.

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Isolation and characterization of a broad pH- and temperature-active, solvent and surfactant stable protease from a new strain of Bacillus subtilis

Cited by 21 publications

References 32 publications

Purification and characterization of trypsin produced by gut bacteria from Anticarsia gemmatalis

Purification and characterization of trypsin produced by gut bacteria from Anticarsia gemmatalis

Production of thermostable multiple enzymes from Bacillus amyloliquefaciens KUB29

Purification, characterization and application of thermoalkaliphilic proteases from Bacillus filamentosus, Lysinibacillus cresolivorans, and Bacillus subtilis

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