Gene Analysis, Expression, and Characterization of an Intracellular α-Amylase from the Extremely Halophilic Archaeon &lt;i&gt;Haloarcula japonica&lt;/i&gt;

Onodera, Manabu; Yatsunami, Rie; Tsukimura, Wataru; Fukui, Toshiaki; Nakasone, Kaoru; Takashina, Tomonori

doi:10.1271/bbb.120693

Cited by 25 publications

(15 citation statements)

References 29 publications

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“…In general, Ca 2+ stimulates the enzyme activity of or stabilizes α-amylases [ 10 , 16 , 30 , 51 , 55 , 57 ]. However, some α-amylases are Ca 2+ insensitive [ 17 , 20 , 32 , 33 , 50 , 56 ]. Furthermore, in a few cases, Ca 2+ inhibits the activity of α-amylase [ 21 , 31 , 58 , 59 ].…”

Section: Resultsmentioning

confidence: 99%

“…Although EDTA and Na 2 EDTA usually act as inhibitors of the activity of α-amylase [ 19 , 48 , 56 , 58 ], in a few cases, EDTA had been noted to stimulate the activity of α-amylase [ 31 , 59 ]. Nevertheless, some α-amylases had been reported to be insensitive to EDTA and Na 2 EDTA [ 20 , 33 , 44 , 50 , 54 , 55 ]. In the present study, TpAA was insensitive to Ca 2+ and EDTA, similar to some α-amylases reported previously [ 20 , 33 , 50 ].…”

Section: Resultsmentioning

confidence: 99%

“…Nevertheless, some α-amylases had been reported to be insensitive to EDTA and Na 2 EDTA [ 20 , 33 , 44 , 50 , 54 , 55 ]. In the present study, TpAA was insensitive to Ca 2+ and EDTA, similar to some α-amylases reported previously [ 20 , 33 , 50 ].…”

Section: Resultsmentioning

confidence: 99%

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Purification and Characterization of a Highly Efficient Calcium-Independent α-Amylase from Talaromyces pinophilus 1-95

et al. 2015

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Alpha-amylase is a very important enzyme in the starch conversion process. Most of the α-amylases are calcium-dependent and exhibit poor performance in the simultaneous saccharification and fermentation process of industrial bioethanol production that uses starch as feedstock. In this study, an extracellular amylolytic enzyme was purified from the culture broth of newly isolated Talaromyces pinophilus strain 1-95. The purified amylolytic enzyme, with an apparent molecular weight of 58 kDa on SDS-PAGE, hydrolyzed maltopentaose, maltohexaose, and maltoheptaose into mainly maltose and maltotriose and minor amount of glucose, confirming the endo-acting mode of the enzyme, and hence, was named Talaromyces pinophilus α-amylase (TpAA). TpAA was most active at pH 4.0–5.0 (with the temperature held at 37°C) and 55°C (at pH 5.0), and stable within the pH range of 5.0–9.5 (at 4°C) and below 45°C (at pH 5.0). Interestingly, the Ca2+ did not improve its enzymatic activity, optimal temperature, or thermostability of the enzyme, indicating that the TpAA was Ca2+-independent. TpAA displayed higher enzyme activity toward malto-oligosaccharides and dextrin than other previously reported α-amylases. This highly active Ca2+-independent α-amylase may have potential applications in starch-to-ethanol conversion process.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Purification and Characterization of a Highly Efficient Calcium-Independent α-Amylase from Talaromyces pinophilus 1-95

et al. 2015

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“…Transformation of Ha. japonica was performed using the polyethylene glycol method (27). Transformants were plated onto agar plates containing pravastatin.…”

Section: Methodsmentioning

confidence: 99%

Complete Biosynthetic Pathway of the C₅₀Carotenoid Bacterioruberin from Lycopene in the Extremely Halophilic Archaeon Haloarcula japonica

Yang¹,

Yatsunami²,

Ando³

et al. 2015

J. Bacteriol.

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Haloarcula japonica, an extremely halophilic archaeon that requires high concentrations of NaCl for growth, accumulates the C 50 carotenoid bacterioruberin (BR). By homology analysis, a gene cluster, including c0507, c0506, and c0505, was found and predicted to be involved in the synthesis of bacterioruberin. To elucidate the function of the encoded enzymes, we constructed Ha. japonica mutants of these genes and analyzed carotenoids produced by the mutants. Our research showed that c0507, c0506, and c0505 encoded a carotenoid 3,4-desaturase (CrtD), a bifunctional lycopene elongase and 1,2-hydratase (LyeJ), and a C 50 carotenoid 2؆,3؆-hydratase (CruF), respectively. The above three carotenoid biosynthetic enzymes catalyze the reactions that convert lycopene to bacterioruberin in Ha. japonica. This is the first identification of functional CrtD and CruF in archaea and elucidation of the complete biosynthetic pathway of bacterioruberin from lycopene. IMPORTANCEHaloarcula japonica, an extremely halophilic archaeon, accumulates the C 50 carotenoid bacterioruberin (BR). In this study, we have identified three BR biosynthetic enzymes and have elucidated their functions. Among them, two enzymes were found in an archaeon for the first time. Our results revealed the biosynthetic pathway responsible for production of BR in Ha. japonica and provide a basis for investigating carotenoid biosynthetic pathways in other extremely halophilic archaea. Elucidation of the carotenoid biosynthetic pathway in Ha. japonica may also prove useful for producing the C 50 carotenoid BR efficiently by employing genetically modified haloarchaeal strains.

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“…salaria H5-DGR. As model organisms, Haloarcula have enormous potential for studying various archaebacterial mechanisms, including archaea-virus interactions (CRISPR-Cas system) (Li et al, 2014), metabolism (bioplastic production, carotenoids, and enzymes) (Camacho et al, 2009;Han et al, 2007;Yatsunami et al, 2014), and genetics (gene characterization and RNA structure) (Mallika and Kundua, 2015;Onodera et al, 2013). Also, as members of the Haloarcula genus have the ability to thrive in extreme high salt environments, most studies of Haloarcula have focused on their dynamic osmo-adaptive strategies (Becker et al, 2014;Miyashita et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Complete genome sequence of Haloarcula sp. CBA1115 isolated from non-purified solar salts

et al. 2015

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Gene Analysis, Expression, and Characterization of an Intracellular α-Amylase from the Extremely Halophilic Archaeon <i>Haloarcula japonica</i>

Cited by 25 publications

References 29 publications

Purification and Characterization of a Highly Efficient Calcium-Independent α-Amylase from Talaromyces pinophilus 1-95

Purification and Characterization of a Highly Efficient Calcium-Independent α-Amylase from Talaromyces pinophilus 1-95

Complete Biosynthetic Pathway of the C₅₀Carotenoid Bacterioruberin from Lycopene in the Extremely Halophilic Archaeon Haloarcula japonica

Complete genome sequence of Haloarcula sp. CBA1115 isolated from non-purified solar salts

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Gene Analysis, Expression, and Characterization of an Intracellular α-Amylase from the Extremely Halophilic Archaeon <i>Haloarcula japonica</i>

Cited by 25 publications

References 29 publications

Purification and Characterization of a Highly Efficient Calcium-Independent α-Amylase from Talaromyces pinophilus 1-95

Purification and Characterization of a Highly Efficient Calcium-Independent α-Amylase from Talaromyces pinophilus 1-95

Complete Biosynthetic Pathway of the C50Carotenoid Bacterioruberin from Lycopene in the Extremely Halophilic Archaeon Haloarcula japonica

Complete genome sequence of Haloarcula sp. CBA1115 isolated from non-purified solar salts

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Complete Biosynthetic Pathway of the C₅₀Carotenoid Bacterioruberin from Lycopene in the Extremely Halophilic Archaeon Haloarcula japonica