Operative utility of salt-stable proteases of halophilic and halotolerant bacteria in the biotechnology sector

Mokashe, Narendra U.; Chaudhari, Bhushan L.; Patil, Ulhas

doi:10.1016/j.ijbiomac.2018.05.217

Cited by 75 publications

(57 citation statements)

References 235 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…As a result of the increase of LAB abundance in Stage III, a significantly increase in pH was observed, which might be mainly caused by the significant increase of basic nitrogenous substances such as ammonia and amines, and it was consistent with the results of RDA analysis that pH was significantly positive correlated with TVB-N ( Figure 4A). Grasshopper sub shrimp paste is a Chinese traditional fermented salted food, its high salinity is not only conducive to the storage of products, but also the most important factor limiting the selection and evolution of microbiota (Mokashe et al, 2018). In the early stages of fermentation, the colony counts showed an upward trend, which was due to the relatively rich nutrients, which were conducive to the growth of bacteria.…”

Section: Discussionmentioning

confidence: 99%

The Impact of Microbial Diversity on Biogenic Amines Formation in Grasshopper Sub Shrimp Paste During the Fermentation

Sang

Zhu

et al. 2020

Front. Microbiol.

View full text Add to dashboard Cite

Biogenic amines (BAs) and microbial diversity are important factors affecting food quality and safety in fermented foods. In this study, the bacterial and fungal diversity in grasshopper sub shrimp paste taken at different fermentation times were comprehensively analyzed, while the pH, colony counts, salinity, total volatile base nitrogen (TVB-N) and BA contents were quantitatively determined. In addition, the correlations among the samples with respect to microbial communities and the different parameters investigated especially BAs were also established. By combining the results of spearman correlation heatmap with the contents of BAs produced by the 102 halotolerant bacteria isolated from the grasshopper sub shrimp paste, six major genera of bacteria (Jeotgalibaca, Jeotgalicoccus, Lysinibacillus, Sporosarcina, Staphylococcus, and Psychrobacter) were found to be positively correlated with BA production level, suggesting that these bacteria might have a strong tendency to produce BAs. Other bacteria such as Lentibacillus, Pseudomonas, and Salinicoccus were considered as poor BA producers. The grasshopper sub shrimp paste was characterized by a relatively high abundance of Tetragenococcus, which was the dominant genus during the fermentation process, and it also produced a relatively high level of BAs but the spearman correlation heatmap revealed a negative correlation between T. muriaticus and BA level. Analysis of the species relevance network in grasshopper sub shrimp explained that the actual production of BAs by a certain strain was closely related to other species present in the complex fermentation system.

show abstract

Section: Discussionmentioning

confidence: 99%

The Impact of Microbial Diversity on Biogenic Amines Formation in Grasshopper Sub Shrimp Paste During the Fermentation

Sang

Zhu

et al. 2020

Front. Microbiol.

View full text Add to dashboard Cite

show abstract

“…On the other hand, secondary metabolites synthetized by microorganisms growing in extreme conditions might also be difficult to obtain in large quantities. It would be therefore interesting to dig deeper in this area, as it has been done elsewhere for other purposes: biotechnological Mokashe et al, 2018), industrial (Sarmiento et al, 2015), pharmaceutical (Irwin, 2010;Karker et al, 2016;Patel, 2016;Oliveira et al, 2018), or ecological (Casillo et al, 2018;Orellana et al, 2018). Finally, Table 4 gives many examples of compounds isolated from different plant species and different tissues from these species.…”

Section: Diversity Of Origins In Natural Compoundsmentioning

confidence: 99%

Unraveling Plant Natural Chemical Diversity for Drug Discovery Purposes

Lautie

Russo

Ducrot³

2020

Front. Pharmacol.

156

120

View full text Add to dashboard Cite

The screening and testing of extracts against a variety of pharmacological targets in order to benefit from the immense natural chemical diversity is a concern in many laboratories worldwide. And several successes have been recorded in finding new actives in natural products, some of which have become new drugs or new sources of inspiration for drugs. But in view of the vast amount of research on the subject, it is surprising that not more drug candidates were found. In our view, it is fundamental to reflect upon the approaches of such drug discovery programs and the technical processes that are used, along with their inherent difficulties and biases. Based on an extensive survey of recent publications, we discuss the origin and the variety of natural chemical diversity as well as the strategies to having the potential to embrace this diversity. It seemed to us that some of the difficulties of the area could be related with the technical approaches that are used, so the present review begins with synthetizing some of the more used discovery strategies, exemplifying some key points, in order to address some of their limitations. It appears that one of the challenges of natural product-based drug discovery programs should be an easier access to renewable sources of plant-derived products. Maximizing the use of the data together with the exploration of chemical diversity while working on reasonable supply of natural product-based entities could be a way to answer this challenge. We suggested alternative ways to access and explore part of this chemical diversity with in vitro cultures. We also reinforced how important it was organizing and making available this worldwide knowledge in an "inventory" of natural products and their sources. And finally, we focused on strategies based on synthetic biology and syntheses that allow reaching industrial scale supply. Approaches based on the opportunities lying in untapped natural plant chemical diversity are also considered.

show abstract

“…In contrast to halophilic enzymes, which tend to be destabilized and inactivated at low-salt concentration due to strong repulsion force exerted by the acidic residues (Chakravorty et al, 2017;Mokashe et al, 2018), protease Als is highly stable and active in the absence of NaCl. It was noticed that protease Als possesses a higher content of basic lysine residues compared with homologous halolysins ( Supplementary Table 3) which commonly contain few lysine residue along with the excess of acidic residues (Mokashe et al, 2018). The abovementioned surface ion pairs, including those involving lysine residues, may contribute to the stabilization of protease Als in the absence of NaCl.…”

Section: Discussionmentioning

confidence: 95%

“…Protease Als possesses an excess of solvent-accessible acidic amino acid residues and displays high halotolerance, as evidenced by the findings that the enzyme exhibited improved activity at 0.5-2.0 M NaCl, maintained approximately 100% of its activity at 3 M NaCl, and showed enhanced thermostability with increasing salt concentration. The possession of an excess of acidic amino acid residues located on protein surface is regarded as an adaptive mechanism of halophilic enzymes, wherein the solvent-accessible acidic residues are involved in the formation of a strong hydration shell to maintain structural stability of halophilic enzymes at high salt concentrations (Mevarech et al, 2000;DasSarma and DasSarma, 2015;Mokashe et al, 2018). Meanwhile, halophilic enzymes could maintain their structural flexibility necessary for catalytic activity at high salinity via the electrostatic repulsion of negatively charged residues, while the hydrophobic core in non-halophilic enzymes would be rigidified in the presence of a high concentration of salts, leading to a decrease of the flexibility required for efficient catalysis (Mevarech et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

“…In addition, subtilases from halophilic/halotolerant microorganisms usually function at high salt concentrations and could occasionally display polyextremotolerant attributes like tolerance to alkaline pH, elevated temperature, and organic solvent etc. (Mokashe et al, 2018); nevertheless, they are less thermostable than their counterparts from thermophiles. The exploration of more robust subtilases with polyextremotolerant attributes is not only scientifically significant for further understanding the mechanism of enzyme adaptation, but it is also of great practical importance in developing proteolytic biocatalysts with a wider versatility to multiple extreme conditions commonly encountered in industrial applications.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Extracellular Production, Characterization, and Engineering of a Polyextremotolerant Subtilisin-Like Protease From Feather-Degrading Thermoactinomyces vulgaris Strain CDF

et al. 2020

View full text Add to dashboard Cite

Here, the gene encoding a subtilisin-like protease (protease Als) was cloned from Thermoactinomyces vulgaris strain CDF and expressed in Escherichia coli. The recombinant enzyme was released into the culture medium of E. coli as a mature form (mAls). Purified mAls displayed optimal activity at 60–70°C and pH 10.0 using azo-casein as the substrate, and showed a half-life of 13.8 h at 70°C. Moreover, the activity of thermostable mAls was comparable to or higher than those of mesophilic subtilisin Carlsberg and proteinase K at low temperatures (10–30°C). Protease Als was also stable in several organic solvents and showed high compatibility with commercial laundry detergents. Notably, mAls exhibited approximately 100% of its activity at 3 M NaCl, and showed enhanced thermostability with the increase of NaCl concentration up to 3 M. Protease Als possesses an excess of solvent-accessible acidic amino acid residues, which may account for the high halotolerance of the enzyme. Compared with homologous protease C2 from the same strain, protease Als exhibits substantially lower activity toward insoluble keratin substrates but efficiently hydrolyzes soluble keratin released from chicken feathers. Additionally, direct substitution of the substrate-binding site of protease Als with that of protease C2 improves its activity against insoluble keratin substrates. By virtue of its polyextremotolerant attribute and kerationolytic capacity, protease Als may find broad applications in various industries such as laundry detergents, food processing, non-aqueous biocatalysis, and feather processing.

show abstract

Operative utility of salt-stable proteases of halophilic and halotolerant bacteria in the biotechnology sector

Cited by 75 publications

References 235 publications

The Impact of Microbial Diversity on Biogenic Amines Formation in Grasshopper Sub Shrimp Paste During the Fermentation

The Impact of Microbial Diversity on Biogenic Amines Formation in Grasshopper Sub Shrimp Paste During the Fermentation

Unraveling Plant Natural Chemical Diversity for Drug Discovery Purposes

Extracellular Production, Characterization, and Engineering of a Polyextremotolerant Subtilisin-Like Protease From Feather-Degrading Thermoactinomyces vulgaris Strain CDF

Contact Info

Product

Resources

About