Production and Characterization of α-Amylase from an Extremely Halophilic Archaeon, Haloferax sp. HA10

Bajpai, Bhakti; Chaudhary, Monika; Saxena, Jyoti

doi:10.17113/ftb.53.01.15.3824

Cited by 25 publications

(31 citation statements)

References 30 publications

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“…According to the present context, the amylase of strain ALA4 was stable towards commercially available detergents, thereby suggesting its suitability in the formulation of detergents. Similar finding was reported by Bajpai et al (2015) with other bacterial species.…”

Section: +supporting

confidence: 92%

Goat dung as a feedstock for hyper-production of amylase from Glutamicibacter arilaitensis strain ALA4

Aarti¹,

Khusro²,

Agastian³

2017

Bioresour. Bioprocess.

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Background:In modern times, bacteria-associated products; especially enzymes are gaining immense interest among worldwide researchers. Among several enzymes, amylases are of great significance in bioprocess engineering. This investigation was aimed to optimize the amylase production from Glutamicibacter arilaitensis strain ALA4 using goat dung as an inexpensive substrate in solid-state fermentation.Results: Amylase production was initially improved by optimizing physical factors and medium components by one factor at a time method. Two-level full factorial design (2 5 factorial matrix) was applied to screen the selected variables using first-order polynomial model. Parameters such as incubation temperature, moisture, starch, and yeast extract affected the amylase activity significantly (P < 0.05). Central composite design at N = 30 was further employed to evaluate the optimum levels of these variables by a second-order polynomial equation. Maximal amylase activity of 4572.53 ± 41.71 U/g was estimated in the goat dung medium supplemented with 100% moisture, 1% (w/w) starch, and 1% (w/w) yeast extract, being incubated at 40 °C. The optimized parameters revealed approximately twofold increment in the amylase yield (R 2 0.9169) with respect to the original medium. The amylase showed stability at high pH and temperature up to 4 h of incubation with residual activities of 52.32 ± 2.2 and 46.12 ± 3.3%, respectively. Additionally, the enzyme revealed resistant property not only towards various metal ions and organic solvents but also surfactants and inhibitors. Most importantly, the amylases obtained from strain ALA4 depicted remarkable tolerance to commercially available various detergents. Conclusions:This study reports first reference on the hyper-production of amylase from G. arilaitensis using goat dung as the low-cost agro-waste medium. G. arilaitensis strain ALA4 may be utilized for wide spread applications in several bioprocess industries due to the high stability of its amylase towards diversified pH, temperature, solvents, surfactants, and detergents.

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Section: +supporting

confidence: 92%

Goat dung as a feedstock for hyper-production of amylase from Glutamicibacter arilaitensis strain ALA4

Aarti¹,

Khusro²,

Agastian³

2017

Bioresour. Bioprocess.

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“…Stability and activity of the enzyme at extreme salt concentration, acidic to alkaline pH, thermophilic temperature, makes it a strong candidate as an industrial biocatalyst. Bajpai et al optimized the culture conditions for extracellular amylase production by halophilic archaeon, Haloferax sp. HA10 on starch agar plate and reported maximum zone at 3 M (17.5%) NaCl, 1 % starch, pH7 and 37 °C indicating highest amylase activity.…”

Section: Resultsmentioning

confidence: 99%

“…Alpha‐amylases from halophilic archaea, are reported to exhibit activities at NaCl concentration as low as 0.5M ( Haloferax sp. HA10) to as high as 5M ( Haloarcula stain 1) with optimum activity in the range of 2–4.3M …”

Section: Resultsmentioning

confidence: 99%

“…The relative enzyme activity started decreasing from pH 7–9, with 64% at pH 8 and 58% at pH 9, of that at pH 6.0. Among the limited studies on α‐amylases from halophilic archaea, to the best of our knowledge, to date, Haloarcula hispanica was the only isolate reported to exhibit optimum activities at acidic pH (pH 5–6) . Recent study on α‐amylases from Haloterrigena turkmenica was reported to exhibit optimum activity at alkaline pH of 8.5 .…”

Section: Resultsmentioning

confidence: 99%

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Alpha-amylase Production by Extremely Halophilic ArchaeonHalococcusStrain GUVSC8

et al. 2019

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Starch hydrolyzing isolate GUVSC8 is obtained from commercial salt crystals of Vedaranyam, Tamil Nadu, India. GUVSC8 is categorized as an extreme halophile based on its growth on complex medium containing 25% (w/v) NaCl. Morphological, chemotaxonomic, and 16S rRNA gene sequencing reveal the cells to be coccus, producing bright orange C‐50 bacterioruberin pigmentation with 95.95% similar to Halococcus hamelinensis DQ017835. The strain GUVSC8 grown in complex medium devoid of starch does not exhibit amylolytic activity, thereby confirming the induction of amylase production in presence of starch. On incubation of the starch with crude enzyme, numerous pores are observed on the starch granules after 24 h of incubation, indicating vigorous degradation and thereby confirming the amylolytic activity. Thin‐layer chromatography (TLC) and liquid chromatography‐electrospray ionization‐mass spectrometry (LC‐ESI‐MS) analysis reveal that the major end product obtained after amylolytic activity are glucose, maltose, maltotriose, maltotetrose, maltopentose, and other maltooligosaccharides, thus confirming it to be an alpha‐amylase. Effects of NaCl, pH, and temperature, on activity of partially purified amylase, reveal best amylase activity at 2M NaCl, pH6, and 45 °C. The amylase is stable and active in presence of divalent cations such as Mg2+, Ni2+, Zn2+, Ca2+, and Co2+. Enzyme activity significantly reduces with Cu2+ and increases in presence of Mn2+. The amylase is characterized as α‐amylase enzyme as it lost 87% of its activity in presence of EDTA. To the best of the author's knowledge, this is the first report on alpha‐amylase production by salt crystal isolate belonging to the genus Halococcus.

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“…HA10 produced an extracellular detergent-stable a-amylase with a molecular mass of 66 kDa in a culture medium containing 3 M NaCl. A partially purified enzyme showed optimal activity at 55 C, pH 6 and 1 M NaCl [225]. In another survey to study amylases, an a-amylase gene from Natronococcus sp.…”

Section: Amylasesmentioning

confidence: 99%

Systematics of haloarchaea and biotechnological potential of their hydrolytic enzymes

et al. 2017

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Halophilic archaea, also referred to as haloarchaea, dominate hypersaline environments. To survive under such extreme conditions, haloarchaea and their enzymes have evolved to function optimally in environments with high salt concentrations and, sometimes, with extreme pH and temperatures. These features make haloarchaea attractive sources of a wide variety of biotechnological products, such as hydrolytic enzymes, with numerous potential applications in biotechnology. The unique trait of haloarchaeal enzymes, haloenzymes, to sustain activity under hypersaline conditions has extended the range of already-available biocatalysts and industrial processes in which high salt concentrations inhibit the activity of regular enzymes. In addition to their halostable properties, haloenzymes can also withstand other conditions such as extreme pH and temperature. In spite of these benefits, the industrial potential of these natural catalysts remains largely unexplored, with only a few characterized extracellular hydrolases. Because of the applied impact of haloarchaea and their specific ability to live in the presence of high salt concentrations, studies on their systematics have intensified in recent years, identifying many new genera and species. This review summarizes the current status of the haloarchaeal genera and species, and discusses the properties of haloenzymes and their potential industrial applications. SYSTEMATICS OF HALOPHILIC ARCHAEAHalophilic micro-organisms are found in the three domains of life, and are extremophiles living in hypersaline environments in the presence of salt (generally NaCl) as a specific requisite for their growth [1]. Hypersaline environments contain higher salt concentrations than seawater (3.5 % total dissolved salts) [2]. According to the optimum NaCl concentration for growth, micro-organisms fall into one of the following categories: extreme halophiles with optimum growth at 15-30 % (2.5-5.2 M) NaCl; moderate halophiles with optimum growth at 3-15 % (0.5-2.5 M) NaCl; slight halophiles with optimum growth at 1-3 % (0.2-0.5 M) NaCl; non-halophiles with optimum growth at less than 1 % (0.2 M) NaCl; and halotolerant micro-organisms which are non-halophiles showing the ability to tolerate high NaCl concentrations [3]. Halophiles can live in hypersaline environments because they are able to sustain osmotic balance. They use two main strategies to withstand the adverse consequences of water loss when exposed to high salt concentrations. The first strategy used by extremely halophilic archaea (haloarchaea) and halophilic anaerobic bacteria such as members of Halanaerobiales is known as the 'salt-in-cytoplasm' strategy, during which salts such as NaCl or KCl accumulate in the cytoplasm at concentrations similar to the extracellular ones [4,5]. Another mechanism to cope with high salt concentrations is the accumulation of organic molecules such as amino acids, sugars and polyols, known as compatible solutes or osmolytes. Compatible solutes are small and highly soluble molecules that can...

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Production and Characterization of α-Amylase from an Extremely Halophilic Archaeon, Haloferax sp. HA10

Cited by 25 publications

References 30 publications

Goat dung as a feedstock for hyper-production of amylase from Glutamicibacter arilaitensis strain ALA4

Goat dung as a feedstock for hyper-production of amylase from Glutamicibacter arilaitensis strain ALA4

Alpha-amylase Production by Extremely Halophilic ArchaeonHalococcusStrain GUVSC8

Systematics of haloarchaea and biotechnological potential of their hydrolytic enzymes

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