Maltose-forming α-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04

Jung, Jong‐Hyun; Seo, Dong Ho; Holden, James F.; Park, Cheon Seok

doi:10.1007/s00253-013-5068-6

Cited by 31 publications

(30 citation statements)

References 33 publications

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“…␣-Amylases capable of producing high levels of maltose from the hydrolysis of starch have been isolated from fungal and bacterial sources, with maltose content ranging from 53% (wt/wt) to greater than 80% (wt/wt); these sources include Rhizopus oryzae (11), Penicillium expansum (12), Thermomonospora curvata (9), Bacillus megaterium G-2 (13), Streptomyces praecox (14), and Pyrococcus sp. strain ST04 (15). The mechanisms to produce high levels of maltose were postulated to involve these ␣-amylases exhibiting significant multimolecular reactions, including condensation and transglycosylation, in addition to their hydrolytic activity (14,(16)(17)(18) or exhibiting an exo-type maltose-forming ␣-amylase action pattern (13,15).…”

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confidence: 99%

“…strain ST04 (15). The mechanisms to produce high levels of maltose were postulated to involve these ␣-amylases exhibiting significant multimolecular reactions, including condensation and transglycosylation, in addition to their hydrolytic activity (14,(16)(17)(18) or exhibiting an exo-type maltose-forming ␣-amylase action pattern (13,15). Saccharifying ␣-amylases, mainly ␣-amylase from Aspergillus oryzae, are used in the industrial production of maltose syrups with a 40 to 50% maltose content (19).…”

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Novel Maltogenic Amylase CoMA from Corallococcus sp. Strain EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose

Zhou

Zhang

et al. 2018

Appl Environ Microbiol

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The gene encoding the novel amylolytic enzyme designated CoMA was cloned from sp. strain EGB. The deduced amino acid sequence contained a predicted lipoprotein signal peptide (residues 1 to 18) and a conserved glycoside hydrolase family 13 (GH13) module. The amino acid sequence of CoMA exhibits low sequence identity (10 to 19%) with cyclodextrin-hydrolyzing enzymes (GH13_20) and is assigned to GH13_36. The most outstanding feature of CoMA is its ability to catalyze the conversion of maltooligosaccharides (≥G3) and soluble starch to maltose as the sole hydrolysate. Moreover, it can hydrolyze γ-cyclodextrin and starch to maltose and hydrolyze pullulan exclusively to panose with relative activities of 0.2, 1, and 0.14, respectively. CoMA showed both hydrolysis and transglycosylation activities toward α-1,4-glycosidic bonds but not to α-1,6-linkages. Moreover, glucosyl transfer was postulated to be the major transglycosidation reaction for producing a high level of maltose without the attendant production of glucose. These results indicated that CoMA possesses some unusual properties that distinguish it from maltogenic amylases and typical α-amylases. Its physicochemical properties suggested that it has potential for commercial development. The α-amylase from sp. EGB, which was classified to the GH13_36 subfamily, can catalyze the conversion of maltooligosaccharides (≥G3) and soluble starch to maltose as the sole hydrolysate. An action mechanism for producing a high level of maltose without the attendant production of glucose has been proposed. Moreover, it also can hydrolyze γ-cyclodextrin and pullulan. Its biochemical characterization suggested that CoMA may be involved the accumulation of maltose in media.

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Novel Maltogenic Amylase CoMA from Corallococcus sp. Strain EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose

Zhou

Zhang

et al. 2018

Appl Environ Microbiol

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“…Recently, we reported a novel exo-type maltose-forming -amylase from Pyrococcus sp. ST04 (Py04_0872; PSMA; Jung et al, 2014). Pyrococcus sp.…”

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confidence: 99%

“…Owing to its unique features such as its substrate specificity for short oligosaccharides, its hydrolysis pattern of dual glycosyl linkages, its hyperthermostability and its optimal activity at low pH, PSMA has considerable potential for industrial application (Jung et al, 2014). To date, maltose production by maltogenic amylase and -amylase has been limited in the starch-processing industry because of the -1,6-linkage of the substrate, which results in the formation of -limited dextrin.…”

Section: Introductionmentioning

confidence: 99%

Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase fromPyrococcussp. ST04

Park

Jung

Park

et al. 2014

Acta Cryst D Biol Crystallogr

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A novel maltose-forming α-amylase (PSMA) was recently found in the hyperthermophilic archaeon Pyrococcus sp. ST04. This enzyme shows <13% amino-acid sequence identity to other known α-amylases and displays a unique enzymatic property in that it hydrolyzes both α-1,4-glucosidic and α-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner. Here, the crystal structure of PSMA at a resolution of 1.8 Å is reported, showing a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1-341) with a typical GH57 family (β/α)7-barrel fold and a C-domain (amino acids 342-597) composed of α-helical bundles. A small closed cavity observed in proximity to the catalytic residues Glu153 and Asp253 at the domain interface has the appropriate volume and geometry to bind a maltose unit, accounting for the selective exo-type maltose hydrolysis of the enzyme. A narrow gate at the putative subsite +1 formed by residue Phe218 and Phe452 is essential for specific cleavage of glucosidic bonds. The closed cavity at the active site is connected to a short substrate-binding channel that extends to the central hole of the tetramer, exhibiting a geometry that is significantly different from classical maltogenic amylases or β-amylases. The structural features of this novel exo-type maltose-forming α-amylase provide a molecular basis for its unique enzymatic characteristics and for its potential use in industrial applications and protein engineering.

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“…1860 (NC_016645) [64,65], Pyrococcus horikoshii OT3 (NC_000961) [66], Pyrococcus sp. ST04 (NC_017946) [67], Pyrococcus yayanosii CH1 (NC_015680) [68], Sulfolobus acidocaldarius DSM 639 (NC_007181) [69], Sulfolobus solfataricus P2 (NZ_LT549890) [70], Thermococcus gammatolerans EJ3 (NC_012804) [71], Thermococcus litoralis DSM 5473 (NC_022084) [72], Thermococcus onnurineus NA1 (NC_011529) [73], Thermococcus sp. CL1 (NC_018015) [74], Thermoplasma acidophilum DSM 1728 (NC_002578) [75,76], Thermoplasma volcanium GSS1 (NC_002689) [77], Vulcanisaeta moutnovskia 768-28 (NC_015151) [78].…”

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Introductory Chapter: A Brief Overview of Archaeal Applications

Sghaier¹,

Najjari²,

Ghedira³

2017

Archaea - New Biocatalysts, Novel Pharmaceuticals and Various Biotechnological Applications

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Additional information is available at the end of the chapter PrologueThe irst member of the Archaea was described in 1880 [1][2][3]. Yet, the recognition and formal description of the domain Archaea, as separated from Bacteria and Eukarya, occurred in 1977 during early phylogenetic analyses based upon ribosomal DNA sequences [4][5][6] The Archaea are ubiquitous in most terrestrial, aquatic and extreme environments (acidophilic, halophilic, mesophilic, methanogenic, psychrophilic and thermophilic) [20,22]. Although very diversiied with a great number of species, luckily, no member of the domain Archaea has been described as a pathogen for humans, animals or plants [23][24][25]. Thus, Archaea are a potentially valuable resource in the development of new biocatalysts, novel pharmaceuticals and various biotechnological applications. Applications of Archaea (for review, see [26][27][28][29][30][31][32] and references therein) may be subdivided into four main ields (Figure 1): (i) commercial enzymes and/or molecules, (ii) environment, (iii) food and (iv) health.

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Maltose-forming α-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04

Cited by 31 publications

References 33 publications

Novel Maltogenic Amylase CoMA from Corallococcus sp. Strain EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose

Novel Maltogenic Amylase CoMA from Corallococcus sp. Strain EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose

Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase fromPyrococcussp. ST04

Introductory Chapter: A Brief Overview of Archaeal Applications

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