Biotechnological Applications of Biocatalysts from the Firmicutes Bacillus and Geobacillus Species

Satyanarayana, T.; Sharma, Archana; Mehta, Deepika; Puri, Akshita; Kumar, Vikash; Mohanan, Nisha; Joshi, Swati

doi:10.1007/978-94-007-2214-9_17

Cited by 17 publications

(5 citation statements)

References 285 publications

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“…A serine protease gene (hspK) of 90 kDa was cloned and sequenced from B. subtilis (Natto) 16 (Yamagata et al, 1995; Satyanarayana et al, 2012; Guleria et al, 2016). A conserved sequence was found between subtilisin BPN and subtilisin Carlsberg from B. amyloliquefaciens and B. licheniformis in the coding region and must have a common precursor (Narhi et al, 1991; Li et al, 2013; Souza et al, 2015).…”

Section: Protease Engineeringmentioning

confidence: 99%

Microbial Proteases Applications

Razzaq

Shamsi

Ali³

et al. 2019

Front. Bioeng. Biotechnol.

423

195

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The use of chemicals around the globe in different industries has increased tremendously, affecting the health of people. The modern world intends to replace these noxious chemicals with environmental friendly products for the betterment of life on the planet. Establishing enzymatic processes in spite of chemical processes has been a prime objective of scientists. Various enzymes, specifically microbial proteases, are the most essentially used in different corporate sectors, such as textile, detergent, leather, feed, waste, and others. Proteases with respect to physiological and commercial roles hold a pivotal position. As they are performing synthetic and degradative functions, proteases are found ubiquitously, such as in plants, animals, and microbes. Among different producers of proteases, Bacillus sp. are mostly commercially exploited microbes for proteases. Proteases are successfully considered as an alternative to chemicals and an eco-friendly indicator for nature or the surroundings. The evolutionary relationship among acidic, neutral, and alkaline proteases has been analyzed based on their protein sequences, but there remains a lack of information that regulates the diversity in their specificity. Researchers are looking for microbial proteases as they can tolerate harsh conditions, ways to prevent autoproteolytic activity, stability in optimum pH, and substrate specificity. The current review focuses on the comparison among different proteases and the current problems faced during production and application at the industrial level. Deciphering these issues would enable us to promote microbial proteases economically and commercially around the world.

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Section: Protease Engineeringmentioning

confidence: 99%

Microbial Proteases Applications

Razzaq

Shamsi

Ali³

et al. 2019

Front. Bioeng. Biotechnol.

423

195

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“…We also identified lanthipeptides coded on genomes of bacterial strains that have not been recognized as lanthipeptide producers. Furthermore, we are paying close attention to the thermophilic Geobacillus , which is seen as a genus with a great biotechnological potential [ 20 ].…”

Section: Introductionmentioning

confidence: 99%

Identification of Putative Novel Class-I Lanthipeptides in Firmicutes: A Combinatorial In Silico Analysis Approach Performed on Genome Sequenced Bacteria and a Close Inspection of Z-Geobacillin Lanthipeptide Biosynthesis Gene Cluster of the Thermophilic Geobacillus sp. Strain ZGt-1

Alkhalili

Canbäck

2018

IJMS

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Lanthipeptides are ribosomally synthesized and post-translationally modified polycyclic peptides. Lanthipeptides that have antimicrobial activity are known as lantibiotics. Accordingly, the discovery of novel lantibiotics constitutes a possible solution for the problem of antibiotic resistance. We utilized the publicly available genome sequences and the bioinformatic tools tailored for the detection of lanthipeptides. We designed our strategy for screening of 252 firmicute genomes and detecting class-I lanthipeptide-coding gene clusters. The designed strategy resulted in identifying 69 class-I lanthipeptide sequences, of which more than 10% were putative novel. The identified putative novel lanthipeptides have not been annotated on the original or the RefSeq genomes, or have been annotated merely as coding for hypothetical proteins. Additionally, we identified bacterial strains that have not been previously recognized as lanthipeptide-producers. Moreover, we suggest corrections for certain firmicute genome annotations, and recommend lanthipeptide records for enriching the bacteriocin genome mining tool (BAGEL) databases. Furthermore, we propose Z-geobacillin, a putative class-I lanthipeptide coded on the genome of the thermophilic strain Geobacillus sp. ZGt-1. We provide lists of putative novel lanthipeptide sequences and of the previously unrecognized lanthipeptide-producing bacterial strains, so they can be prioritized for experimental investigation. Our results are expected to benefit researchers interested in the in vitro production of lanthipeptides.

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“…These genera belong to the family Bacillaceae , order Bacillales , and phylum Firmicutes ; they are recognized for their ability to form endospores and are commonly found in various soil environments [ 1 ]. It is important to note that some members of the phylum Firmicutes are industrially valuable for the development of different biotechnological products, like antibiotics, enzymes, and dairy products [ 57 , 58 ]. In this research, the demonstrated ability of these microorganisms to produce hydrolytic enzymes highlights the significance of further characterizing these isolates for their biotechnological use.…”

Section: Discussionmentioning

confidence: 99%

Isolation of Thermophilic Bacteria from Extreme Environments in Northern Chile

Valenzuela,

Solís-Cornejo,

Araya

et al. 2024

Microorganisms

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The northern region of Chile boasts unique geographical features that support the emergence of geothermal effluents, salt lagoons, and coastal creeks. These extreme climate conditions create polyextreme habitats for microorganisms, particularly adapted to survive these harsh environments. These extremophilic microorganisms hold immense potential as a source of hydrolytic enzymes, among other biotechnological applications. In this study, we isolated 15 strains of aerobic thermophilic bacteria (45–70 °C) from sediment samples collected at five different ecological sites, including hot springs, geothermal fields, and lagoons in the Atacama Desert and Andes high planes. Analyses of the 16S rRNA gene sequences of the isolates showed a close genetic similarity (98–100%) with microorganisms of the genera Parageobacillus, Geobacillus, Anoxybacillus, and Aeribacillus. Notably, these thermophiles exhibited significant hydrolytic enzyme activity, particularly amylases, lipases, and proteases. These findings underscore the potential of using these thermophilic bacterial strains as an invaluable source of thermozymes with wide-ranging applications in diverse industries, such as detergent formulations, pharmaceutical processing, and food technology. This research highlights the ecological significance of these extreme environments in the Atacama Desert and Andes high plains, which serve as vital ecological niches housing extremophilic bacteria as a genetic source of relevant thermozymes, promising great potential for innovation in the biotechnology industry.

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Biotechnological Applications of Biocatalysts from the Firmicutes Bacillus and Geobacillus Species

Cited by 17 publications

References 285 publications

Microbial Proteases Applications

Microbial Proteases Applications

Identification of Putative Novel Class-I Lanthipeptides in Firmicutes: A Combinatorial In Silico Analysis Approach Performed on Genome Sequenced Bacteria and a Close Inspection of Z-Geobacillin Lanthipeptide Biosynthesis Gene Cluster of the Thermophilic Geobacillus sp. Strain ZGt-1

Isolation of Thermophilic Bacteria from Extreme Environments in Northern Chile

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