Molecular bases of protein halotolerance

Graziano, Giuseppe; Merlino, Antonello

doi:10.1016/j.bbapap.2014.02.018

Cited by 100 publications

(105 citation statements)

References 81 publications

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“…Moderately halophilic SRB have repeatedly been reported, such as Desulfohalobium utahense isolated from sediments of the Great Salt Lake ( Jakobsen, Kjeldsen, & Ingvorsen, 2006) and Desulfovibrio bastinii originating from deep subsurface oilfield water (Magot, Basso, Tardy-Jacquenod, & Caumette, 2004). The physiological and molecular mechanisms of adaptation to high salinity, i.e., homeostasis, DNA and protein structures (Graziano & Merlino, 2014;Paul, Bag, Das, Harvill, & Dutta, 2008), have thus far not been studied in detail with SRB.…”

Section: Piezophilesmentioning

confidence: 97%

A Post-Genomic View of the Ecophysiology, Catabolism and Biotechnological Relevance of Sulphate-Reducing Prokaryotes

Rabus

Venceslau

Wöhlbrand

et al. 2015

Advances in Microbial Physiology

253

286

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Section: Piezophilesmentioning

confidence: 97%

A Post-Genomic View of the Ecophysiology, Catabolism and Biotechnological Relevance of Sulphate-Reducing Prokaryotes

Rabus

Venceslau

Wöhlbrand

et al. 2015

Advances in Microbial Physiology

253

286

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“…However, there are also numerous proteins that tolerate high salt concentrations, which are not isolated from halophilic sources. These proteins are defined as halotolerants (Graziano & Merlino, 2014). Halotolerant enzymes remain active over a broad range of NaCl concentration, without any specific salt dependence.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a halotolerant lipase from the lactic acid bacteria Lactobacillus plantarum useful in food fermentations

Esteban-Torres

Mancheño

Rivas

et al. 2015

LWT - Food Science and Technology

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a b s t r a c tLactobacillus plantarum is a lactic acid bacteria found in fermented foods on which high salt concentrations are present. So far, no salt-tolerant lipase has been described from lactic acid bacteria. In the present study, the gene lp_3562 encoding a putative esterase/lipase was cloned and expressed in Escherichia coli BL21 (DE3) and the overproduced Lp_3562 protein has been biochemically characterized. Lp_3562 is a lipase active on tributyrin and also on other long chain substrates. Although the highest activity was observed at pH 7, the enzyme showed activity at pH 5.0e8.0. Lp_3562 exhibited optimal lipase activity at 40 C and, showing more than 40% of maximal activity at refrigeration temperature (5 C). Conversely, Lp_3562 presented good thermostability exhibiting more than 80% of its maximal activity after 20 h incubation at 45 C. More interestingly, Lp_3562 was active under NaCl concentrations higher than 20%. The biochemical properties exhibited by Lp_3562 make this halotolerant lipase attractive for its use in food fermentations.

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“…Halophilic proteins generally contain more surface acidic charges than mesophilic proteins to get activated or stabilized in hypersaline solutions [24]. However, halotolerant proteins can adapt to a wide range of salt concentrations and probably possess similar surface charges to mesophilic proteins.…”

Section: Discussionmentioning

confidence: 99%

“…Moderate concentrations of salt (1-3 M) can enhance the activity and thermal stability of dCAs but salt is not essential for their activity and folding. Structural studies have led to the proposal that the surface electrostatic property is crucial to the halotolerance of dCAS as well as the other halotolerant proteins [23,24] The low intracellular ion strength suggests that it might be unnecessary for the intracellular Dunaliella proteins to be halotolerant. However, an early study indicated that enzymes in the crude extracts of Dunaliella parva exhibit a broad range of NaCl sensitivity from 100 mM to molar level [25].…”

Section: Q2mentioning

confidence: 99%