Production of ?-amylase fromHalobacterium halobium

Patel, S. R.; Jain, Nisha; Madamwar, Datta

doi:10.1007/bf00656510

Cited by 18 publications

(11 citation statements)

References 6 publications

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“…The amylase production in the presence of soluble starch has been reported to accelerate in extremely halophilic archaea, Halobacterium salinarum (formerly Halobacterium halobium ), and Natronococcus sp. strain Ah‐36, indicating starch to be the best inducer . Similarly, moderately halophilic bacteria Halomonas meridian and Micrococcus sp.…”

Section: Resultsmentioning

confidence: 95%

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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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Section: Resultsmentioning

confidence: 95%

“…strain Ah-36, indicating starch to be the best inducer. [44,17] Similarly, moderately halophilic bacteria Halomonas meridian and Micrococcus sp. are reported to produce amylase only in the presence of starch.…”

Section: Inductive Mode Of Amylase Productionmentioning

confidence: 99%

Alpha-amylase Production by Extremely Halophilic ArchaeonHalococcusStrain GUVSC8

et al. 2019

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“…S‐1 has a high tolerance to organic solvents 43. However, there are few reports on pure halophilic amylases, only those isolated from halophilic bacteria such as Haloferax mediterranei, Halobacterium salinarum and Natrococcus amylolyticus 44–48. On the other hand, it has been reported that the amylase from Nesterenkonia halobia shows maximum production in 48 h at a concentration of 1–2 mol L −1 NaCl.…”

Section: Halophilic Enzymesmentioning

confidence: 99%

Halophilic hydrolases as a new tool for the biotechnological industries

et al. 2012

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Halophilic micro-organisms are able to survive in high salt concentrations because they have developed diverse biochemical, structural and physiological modifications, allowing the catalytic synthesis of proteins with interesting physicochemical and structural properties. The main characteristic of halophilic enzymes that allows them to be considered as a novel alternative for use in the biotechnological industries is their polyextremophilicity, i.e. they have the capacity to be thermostable, tolerate a wide range of pH, withstand denaturation and tolerate high salt concentrations. However, there have been relatively few studies on halophilic enzymes, with some being based on their isolation and others on their characterisation. These enzymes are scarcely researched because attention has been focused on other extremophile micro-organisms. Only a few industrial applications of halophilic enzymes, principally in the fermented food, textile, pharmaceutical and leather industries, have been reported. However, it is important to investigate applications of these enzymes in more biotechnological processes at both the chemical and the molecular level. This review discusses the modifications of these enzymes, their industrial applications and research perspectives in different biotechnological areas.

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“…(Onishi and Hidaka 1978) where they are secreted in a medium containing sodium chloride or potassium chloride and require these salts for their activity. Halophilic amylase has also been reported from Halobacterrum halobzum (Good and Hartman 1970;Patel et al 1993).…”

Section: Introductionmentioning

confidence: 91%

Production of moderately halophilic amylase by newly isolated Micrococcus sp. 4 from a salt-pan

Khire

1994

Lett Appl Microbiol

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A new moderately halophilic Micrococcus sp. 4, isolated from salt‐pan water from India, produced extracellular amylase when cultivated aerobically in medium containing wheat bran, peptone, beef extract and sodium chloride. Other salts, such as sodium nitrate, potassium nitrate and sodium sulphate, were also found to be suitable for growth and enzyme production. Maximum amylase activity (1.2 IU ml‐1) was secreted in the presence of 1 mol 1‐1 sodium chloride. The enzyme requires the presence of either sodium chloride, potassium chloride, sodium nitrate, sodium citrate or sodium acetate for its activity. Maximum activity was found in the presence of 1 mol 1‐1 sodium chloride. The pH and temperature optima for enzyme activity were 7.5 and 50°C, respectively.

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Production of ?-amylase fromHalobacterium halobium

Cited by 18 publications

References 6 publications

Alpha-amylase Production by Extremely Halophilic ArchaeonHalococcusStrain GUVSC8

Alpha-amylase Production by Extremely Halophilic ArchaeonHalococcusStrain GUVSC8

Halophilic hydrolases as a new tool for the biotechnological industries

Production of moderately halophilic amylase by newly isolated Micrococcus sp. 4 from a salt-pan

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