Biotechnological Aspects of Cold-Active Enzymes

Barroca, Mário Jorge Faria; Santos, Gustavo Oliveira dos; Gerday, Charles; Collins, Tony

doi:10.1007/978-3-319-57057-0_19

Cited by 22 publications

(21 citation statements)

References 59 publications

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“…Increasing protein stability and avoiding aggregation are the fundamental issues for the development of efficient and robust biocatalysts for industrial applications [5,31]. Protein aggregation at elevated temperatures is usually explained by the partial unfolding of the protein molecules and concomitant interactions between newly exposed hydrophobic regions [32][33][34].…”

Section: Discussionmentioning

confidence: 99%

“…Cold-active enzymes represent a promising resource for biotechnological applications since they potentially allow avoiding energy loss for the heating of the reaction mixture and inactivation of the heat-labile compounds [1][2][3][4][5]. Therefore, the rapidly growing number of the cold-active enzymes has been obtained to date using the available genomic sequences of the cold-adapted microorganisms and metagenomic approaches [6,7].…”

Section: Introductionmentioning

confidence: 99%

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Thermal Inactivation of a Cold-Active Esterase PMGL3 Isolated from the Permafrost Metagenomic Library

et al. 2019

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PMGL3 is a cold-adapted esterase which was recently isolated from the permafrost metagenomic library. It exhibits maximum activity at 30 °C and low stability at elevated temperatures (40 °C and higher). Sequence alignment has revealed that PMGL3 is a member of the hormone-sensitive lipase (HSL) family. In this work, we demonstrated that incubation at 40 °C led to the inactivation of the enzyme (t1/2 = 36 min), which was accompanied by the formation of tetramers and higher molecular weight aggregates. In order to increase the thermal stability of PMGL3, its two cysteines Cys49 and Cys207 were substituted by the hydrophobic residues, which are found at the corresponding positions of thermostable esterases from the HSL family. One of the obtained mutants, C207F, possessed improved stability at 40 °C (t1/2 = 169 min) and increased surface hydrophobicity, whereas C49V was less stable in comparison with the wild type PMGL3. Both mutants exhibited reduced values of Vmax and kcat, while C207F demonstrated increased affinity to the substrate, and improved catalytic efficiency.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Thermal Inactivation of a Cold-Active Esterase PMGL3 Isolated from the Permafrost Metagenomic Library

et al. 2019

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“…Twenty-two isolates were positive for all the three enzymes under consideration. While the enzymes produced by cold-adapted microorganisms are considered to play an important role in the survival of these organisms under temperature stress, they are also making their way to biotechnological industries with economic advantages [2,8]. Among the bacteria under study, Pseudomonas proteolytica has been reported to produce cold-active lipase [17].…”

Section: Bioprospection Of Psychrotolerant Bacteriamentioning

confidence: 99%

“…Psychrotolerant bacteria, along with their ability to adapt to the temperatures close to or below freezing, require specific strategies for the continuance of their metabolic activities including maintenance of the membrane fluidity and the protein synthesis at low temperature. Furthermore, the psychrotolerant bacteria and their cold-active enzymes are being focused for their importance in biotechnological applications and physiological adaptations [1,2,26,41].…”

Section: Introductionmentioning

confidence: 99%

16S rRNA gene sequencing and MALDI-TOF mass spectrometry based comparative assessment and bioprospection of psychrotolerant bacteria isolated from high altitudes under mountain ecosystem

et al. 2019

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The Himalayan Mountains are placed among the globally recognized biodiversity hot spots. While the Indian Himalayan Region (IHR) has been subjected to extensive studies on plant and animal biodiversity, microbial diversity is now being studied for its bioprospection. The present paper deals with the evaluation of bacterial diversity in high-altitude soil samples from IHR following polyphasic approach including comparison between the MALDI-TOF mass spectrometry and 16S rRNA gene sequencing for species-level identification. Initially, a culture collection of large number of bacterial isolates was established in the laboratory. Performing morphological and biochemical screenings, sixty-one representative isolates were selected for mass spectrometry and gene sequencing. Both the methods emerged with bacterial identification showing maximum number of Bacillus followed by Pseudomonas species. The other frequently isolated strains belonged to the genera Alcaligenes, Carnobacterium, Lysinibacillus, Microbacterium, Paenarthrobacter, Rhodococcus, Serratia and Stenotrophomonas. Although the MALDI-TOF technique appeared to be advantageous as less time-consuming in comparison with 16S rRNA-based method, the discrepancies at species level indicated the limited database of MALDI Biotyper and species complexity in the genera. The remarkable characteristics of the bacterial isolates were their tolerance to wide range of pH and temperature. Their potential to produce industrially valuable enzymes indicated their importance in bioprospection. Accessioning of these bacterial isolates in microbial culture collections is a cautious effort for their availability to conduct advanced research on these cold-adapted bacteria in future.

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“…To this end, heat-labile enzymes have great potential, as heat inactivation can be performed at temperatures that do not cause the melting of double-stranded DNA (dsDNA), eliminating the need for additional chemical extraction steps [77]. The detergent, biofuel production and pulp and paper industries are also interested in cold-active hydrolases, such as proteases, lipases, amylases and cellulases, as these enzymes can provide economic benefits by reducing energy consumption and production costs [80,81].…”

Section: Deep-sea Psychrophilic Enzymesmentioning

confidence: 99%

Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review

et al. 2019

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The deep sea, which is defined as sea water below a depth of 1000 m, is one of the largest biomes on the Earth, and is recognised as an extreme environment due to its range of challenging physical parameters, such as pressure, salinity, temperature, chemicals and metals (such as hydrogen sulphide, copper and arsenic). For surviving in such extreme conditions, deep-sea extremophilic microorganisms employ a variety of adaptive strategies, such as the production of extremozymes, which exhibit outstanding thermal or cold adaptability, salt tolerance and/or pressure tolerance. Owing to their great stability, deep-sea extremozymes have numerous potential applications in a wide range of industries, such as the agricultural, food, chemical, pharmaceutical and biotechnological sectors. This enormous economic potential combined with recent advances in sampling and molecular and omics technologies has led to the emergence of research regarding deep-sea extremozymes and their primary applications in recent decades. In the present review, we introduced recent advances in research regarding deep-sea extremophiles and the enzymes they produce and discussed their potential industrial applications, with special emphasis on thermophilic, psychrophilic, halophilic and piezophilic enzymes.Nearly three-quarters of the Earth's surface area is covered by ocean, the average depth of which is 3800 m, implying that the vast majority of our planet comprises deep-sea environments. The deep sea is one of the most mysterious and unexplored environments on the Earth, and it supports diverse microbial communities that play important roles in biogeochemical cycles [1]. The deep sea is also recognised as an extreme environment, as it is characterised by the absence of sunlight and the presence of predominantly low temperatures and high hydrostatic pressures, and these environmental conditions become even more challenging in particular habitats, such as deep-sea hydrothermal vents with their extremely high temperatures of >400 • C, deep hypersaline anoxic basins (DHABs) with their extremely high salinities and abysses of up to 11 km depth with their extremely high pressures.Deep-sea extremophiles are living organisms that can survive and proliferate in deep-sea environments that have extreme physical (pressure and temperature) and geochemical (pH, salinity and redox potential) conditions that are lethal to other organisms. The majority of deep-sea extremophiles belong to the prokaryotes, which are microorganisms in the domains of Archaea and Bacteria [2,3].These extremophilic microorganisms are functionally diverse and widely distributed in taxonomy [4], and they are classified into thermophiles (55 • C to 121 • C), psychrophiles (−2 • C to 20 • C), halophiles (2-5 M NaCl or KCl), piezophiles (>500 atmospheres), alkalophiles (pH > 8), acidophiles (pH < 4) and metalophiles (high concentrations of metals, e.g., copper, zinc, cadmium and arsenic) according to the extreme environments in which they grow and the extreme conditions they can tolerate. Ma...

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Biotechnological Aspects of Cold-Active Enzymes

Cited by 22 publications

References 59 publications

Thermal Inactivation of a Cold-Active Esterase PMGL3 Isolated from the Permafrost Metagenomic Library

Thermal Inactivation of a Cold-Active Esterase PMGL3 Isolated from the Permafrost Metagenomic Library

16S rRNA gene sequencing and MALDI-TOF mass spectrometry based comparative assessment and bioprospection of psychrotolerant bacteria isolated from high altitudes under mountain ecosystem

Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review

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