Differences and similarities in enzymes from the neopullulanase subfamily isolated from thermophilic species

Karlsson, Eva Nordberg; Labes, Antje; Turner, Pernilla; Friðjónsson, Ólafur H.; Wennerberg, Christina; Pozzo, Tania; Hreggvidson, Gudmundur O.; Kristjánsson, Jakob K.; Schönheit, Peter

doi:10.2478/s11756-008-0171-3

Cited by 11 publications

(1 citation statement)

References 19 publications

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“…In a study of new neopullulanase-like GH13 members (neopullulanases, maltogenic amylases, cyclodextrinases) enzymatic and oligomerisation properties were described for enzymes recombinantly produced in E. coli and originating from six genes cloned from the thermophilic bacteria Anoxybacillus, Thermoactinomyces, and Geobacillus or environmental DNA of Icelandic hot springs (Turner et al 2005;Nordberg Karlsson et al 2008). Five of the enzymes had the typical N-terminal domain of neopullulanase-like enzymes, which is involved in dimerisation (Kim et al 2001), while one enzyme originating from environmental DNA lacked the N-terminal domain.…”

Section: Functional Diversity Of Selected Gh13 and Gh57 Membersmentioning

confidence: 99%

An enzyme family reunion — similarities, differences and eccentricities in actions on α-glucans

et al. 2008

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α-Glucans in general, including starch, glycogen and their derived oligosaccharides are processed by a host of more or less closely related enzymes that represent wide diversity in structure, mechanism, specificity and biological role. Sophisticated three-dimensional structures continue to emerge hand-in-hand with the gaining of novel insight in modes of action. We are witnessing the "test of time" blending with remaining questions and new relationships for these enzymes. Information from both within and outside of ALAMY 3 Symposium will provide examples on what the family contains and outline some future directions. In 2007 a quantum leap crowned the structural biology by the glucansucrase crystal structure. This initiates the disclosure of the mystery on the organisation of the multidomain structure and the "robotics mechanism" of this group of enzymes. The central issue on architecture and domain interplay in multidomain enzymes is also relevant in connection with the recent focus on carbohydrate-binding domains as well as on surface binding sites and their long underrated potential. Other questions include, how different or similar are glycoside hydrolase families 13 and 31 and is the lid finally lifted off the disguise of the starch lyase, also belonging to family 31? Is family 57 holding back secret specificities? Will the different families be sporting new "eccentric" functions, are there new families out there, and why are crystal structures of "simple" enzymes still missing? Indeed new understanding and discovery of biological roles continuously emphasize value of the collections of enzyme models, sequences, and evolutionary trees which will also be enabling advancement in design for useful and novel applications.

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Section: Functional Diversity Of Selected Gh13 and Gh57 Membersmentioning

confidence: 99%

An enzyme family reunion — similarities, differences and eccentricities in actions on α-glucans

et al. 2008

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Characteristics, protein engineering and applications of microbial thermostable pullulanases and pullulan hydrolases

Mohanan

Satyanarayana

2016

Appl Microbiol Biotechnol

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Pullulan hydrolyzing enzymes are endoacting, classified based on the substrate specificity and hydrolysis products as pullulanases (type I and II) and pullulan hydrolases (type I, II and III). Pullulanases and pullulan hydrolase type I are produced by bacteria and archaea. Among bacteria, many mesophilic, thermophilic and hyperthermophilic bacteria produce pullulanases and neopullulanases. While pullulan hydrolase type II and type III are produced by fungi and archaea, respectively. These are multi-domain proteins with three conserved catalytic acidic residues of the glycosyl hydrolases. The recent advances in molecular biology and protein engineering via mutagenesis and truncation led to improvement in thermostability, catalytic activity and substrate specificity. Pullulanases are debranching enzymes, which are widely employed in starch saccharification that minimizes the use of glucoamylase (approx. 50 %) and reduces the total reaction time of the industrial starch conversion process. The thermostable amylopullulanases are useful in one-step starch liquefaction and saccharification, which replaces amylolytic enzymes like α-amylase and glucoamylase, thus resulting in the reduction in the cost of sugar production. The enzymes also find application in making resistant starches and as an antistale in bread making. Panose and isopanose containing syrups are useful as prebiotics, while panose has also been reported to display anticarcinogenic activity. This review focuses on the distinguishing features of these enzymes based on the analysis of amino acid sequences and domain structure, besides highlighting recent advances in the molecular biology and protein engineering for enhancing their thermostability, catalytic activity and substrate specificity. This review also briefly summarizes the potential applications of pullulanases and pullulan hydrolases.

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Mining thermophiles for biotechnologically relevant enzymes: evaluating the potential of European and Caucasian hot springs

Burkhardt,

Baruth,

Neele Meyer-Heydecke

et al. 2023

Extremophiles

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The development of sustainable and environmentally friendly industrial processes is becoming very crucial and demanding for the rapid implementation of innovative bio-based technologies. Natural extreme environments harbor the potential for discovering and utilizing highly specific and efficient biocatalysts that are adapted to harsh conditions. This review focuses on extremophilic microorganisms and their enzymes (extremozymes) from various hot springs, shallow marine vents, and other geothermal habitats in Europe and the Caucasus region. These hot environments have been partially investigated and analyzed for microbial diversity and enzymology. Hotspots like Iceland, Italy, and the Azores harbor unique microorganisms, including bacteria and archaea. The latest results demonstrate a great potential for the discovery of new microbial species and unique enzymes that can be explored for the development of Circular Bioeconomy.Different screening approaches have been used to discover enzymes that are active at extremes of temperature (up 120 °C), pH (0.1 to 11), high salt concentration (up to 30%) as well as activity in the presence of solvents (up to 99%). The majority of published enzymes were revealed from bacterial or archaeal isolates by traditional activity-based screening techniques. However, the latest developments in molecular biology, bioinformatics, and genomics have revolutionized life science technologies. Post-genomic era has contributed to the discovery of millions of sequences coding for a huge number of biocatalysts. Both strategies, activity- and sequence-based screening approaches, are complementary and contribute to the discovery of unique enzymes that have not been extensively utilized so far.

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Differences and similarities in enzymes from the neopullulanase subfamily isolated from thermophilic species

Cited by 11 publications

References 19 publications

An enzyme family reunion — similarities, differences and eccentricities in actions on α-glucans

An enzyme family reunion — similarities, differences and eccentricities in actions on α-glucans

Characteristics, protein engineering and applications of microbial thermostable pullulanases and pullulan hydrolases

Mining thermophiles for biotechnologically relevant enzymes: evaluating the potential of European and Caucasian hot springs

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