Improvements of thermophilic enzymes: From genetic modifications to applications

Han, Huawen; Ling, Zhenmin; Khan, Aman; Virk, Amanpreet Kaur; Kulshrestha, Saurabh; Li, Xiangkai

doi:10.1016/j.biortech.2019.01.087

Cited by 83 publications

(32 citation statements)

References 126 publications

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“…Particular interest on industrial applications of extremophiles emerges during the past few decades, because they are able to produce novel biocatalysts functioning under extreme conditions, resulting in unique products and higher production efficiency [65]. Thermozymes offer unique characteristics, such as temperature, chemical, and pH stability, resulting to technological interest in diverse industrial applications, including food, pharmaceutical, chemical, paper, textile processing, biofuel production, pulp, and waste treatment [91]. Consequently, thermophilic bacteria are a good source of novel catalysts suggesting new application or improving the existing processes of industrial interest [92].…”

Section: G33 24g17mentioning

confidence: 99%

Diversity and enzymatic potential of thermophilic bacteria associated with terrestrial hot springs in Algeria

et al. 2020

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This study aims to determine the diversity of culturable thermophilic bacteria isolated from eight terrestrial hot springs in Northeastern of Algeria using the conventional methods, SDS-PAGE fingerprinting of whole-cell proteins and 16S rRNA gene sequencing. In addition, their hydrolytic enzyme activities were also investigated. A total of 293 strains were isolated from the hot springs' water and sediment using different culture media. Overall, five distinct bacterial groups were characterized by whole-cell protein pattern analysis. Based on the 16S rRNA gene sequencing of 100 selected strains, the isolates were assigned to the following three major phyla: Firmicutes (93%), Deinococcus-Thermus (5%), and Actinobacteria (2%), which included 27 distinct species belonging to 12 different phylotypes, Aeribacillus, Aneurinibacillus, Anoxybacillus, Bacillus, Brevibacillus, Geobacillus, Laceyella, Meiothermus, Saccharomonospora, Thermoactinomyces, Thermobifida, and Thermus. The screening for nine extracellular enzymes showed that 65.87% of the isolates presented at least five types of enzyme activities, and 6.48% of strains combined all tested enzymes (amylase, cellulase, pectinase, esculinase, protease, gelatinase, lipase, lecithinase, and nuclease). It was found that Bacillus, Anoxybacillus, Aeribacillus, and Aneurinibacillus were the genera showing the highest activities. Likewise, the study showed an abundant and diverse thermophilic community with novel taxa presenting a promising source of thermozymes with important biotechnological applications. This study showed that a combined identification method using SDS-PAGE profiles of whole-cell proteins and subsequent 16S rRNA gene sequence analysis could successfully differentiate thermophilic bacteria from Algerian hot springs.

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Section: G33 24g17mentioning

confidence: 99%

Diversity and enzymatic potential of thermophilic bacteria associated with terrestrial hot springs in Algeria

et al. 2020

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“…On the other hand, the demand for enzymes that can resist harsh conditions for industrial processes has encouraged the search for enzymes obtained from microorganisms that live in extreme conditions and non-conventional environments (e.g., pH, salinity, temperature, pressure, or radiation) [48][49][50][51][52]. These microorganisms, called extremophiles, produce enzymes capable of catalyzing reactions under non-conventional conditions [53][54][55].…”

Section: Introductionmentioning

confidence: 99%

Modulation of the Biocatalytic Properties of a Novel Lipase from Psychrophilic Serratia sp. (USBA-GBX-513) by Different Immobilization Strategies

et al. 2021

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In this work, the effect of different immobilization procedures on the properties of a lipase obtained from the extremophilic microorganism Serratia sp. USBA-GBX-513, which was isolated from Paramo soils of Los Nevados National Natural Park (Colombia), is reported. Different Shepharose beads were used: octyl-(OC), octyl-glyoxyl-(OC-GLX), cyanogen bromide (BrCN)-, and Q-Sepharose. The performance of the different immobilized extremophile lipase from Serratia (ESL) was compared with that of the lipase B from Candida antarctica (CALB). In all immobilization tests, hyperactivation of ESL was observed. The highest hyperactivation (10.3) was obtained by immobilization on the OC support. Subsequently, the thermal stability at pH 5, 7, and 9 and the stability in the presence of 50% (v/v) acetonitrile, 50% dioxane, and 50% tetrahydrofuran solvents at pH 7 and 40 °C were evaluated. ESL immobilized on octyl-Sepharose was the most stable biocatalyst at 90 °C and pH 9, while the most stable preparation at pH 5 was ESL immobilized on OC-GLX-Sepharose supports. Finally, in the presence of 50% (v/v) tetrahydrofuran (THF) or dioxane at 40 °C, ESL immobilized on OC-Sepharose was the most stable biocatalyst, while the immobilized preparation of ESL on Q-Sepharose was the most stable one in 40% (v/v) acetonitrile.

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“…These enzymes possess various adaptive strategies that help them to function in high temperature. These adaptive strategies are very well covered in the review of Han et al (2019) and Kumar et al (2019). These types of natural thermophilic PET hydrolases thus could efficiently be used for the management of PET wastes.…”

Section: Screening and Sourcing Of Heat-stable Enzymes From Hyperthermentioning

confidence: 99%

Enzymatic Remediation of Polyethylene Terephthalate (PET)–Based Polymers for Effective Management of Plastic Wastes: An Overview

Maurya

Bhattacharya

Khare

2020

Front. Bioeng. Biotechnol.

130

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Globally, plastic-based pollution is now recognized as one of the serious threats to the environment. Among different plastics, polyethylene terephthalate (PET) occupies a pivotal place, its excess presence as a waste is a major environmental concern. Mechanical, thermal, and chemical-based treatments are generally used to manage PET pollution. However, these methods are usually expensive or generate secondary pollutants. Hence, there is a need for a cost-effective and environment-friendly method for efficient management of PET-based plastic wastes. Considering this, enzymatic treatment or recycling is one of the important methods to curb PET pollution. In this regard, PET hydrolases have been explored for the treatment of PET wastes. These enzymes act on PET and end its breakdown into monomeric units and subsequently results in loss of weight. However, various factors, specifically PET crystallinity, temperature, and pH, are known to affect this enzymatic process. For effective hydrolysis of PET, high temperature is required, which facilitates easy accessibility of substrate (PET) to enzymes. However, to function at this high temperature, there is a requirement of thermostable enzymes. The thermostability could be enhanced using glycosylation, immobilization, and enzyme engineering. Furthermore, the use of surfactants, additives such as Ca 2+ , Mg 2+ , and hydrophobins (cysteine-rich proteins), has also been reported to enhance the enzymatic PET hydrolysis through facilitating easy accessibility of PET polymers. The present review encompasses a brief overview of the use of enzymes toward the management of PET wastes. Various methods affecting the treatment process and different constraints arising thereof are also systematically highlighted in the review.

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Improvements of thermophilic enzymes: From genetic modifications to applications

Cited by 83 publications

References 126 publications

Diversity and enzymatic potential of thermophilic bacteria associated with terrestrial hot springs in Algeria

Diversity and enzymatic potential of thermophilic bacteria associated with terrestrial hot springs in Algeria

Modulation of the Biocatalytic Properties of a Novel Lipase from Psychrophilic Serratia sp. (USBA-GBX-513) by Different Immobilization Strategies

Enzymatic Remediation of Polyethylene Terephthalate (PET)–Based Polymers for Effective Management of Plastic Wastes: An Overview

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