Characterization of a thermostable raw-starch hydrolyzing α-amylase from deep-sea thermophile Geobacillus sp.

Jiang, Tao; Cai, Menghao; Huang, Mengmeng; He, Hao; Lu, Jian; Zhou, Xiangshan; Zhang, Yuanxing

doi:10.1016/j.pep.2015.06.002

Cited by 50 publications

(28 citation statements)

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“…For example, the activity of α-amylase from Geobacillus sp. isolated from the sub-seafloor sediments is optimum at 60-65 °C (Jiang et al, 2015). Meanwhile, α-amylase from B. mojovensis isolated from hot spring has optimum activity at 80-90 °C (Sudan et al, 2018;Wu et al, 2018).…”

Section: Effect Of Temperature Ph and Organic Solventmentioning

confidence: 99%

“…While the exploration of new microorganisms from extreme environments to produce more stable enzymes has been done for many years, studies to find new α-amylases continue being carried out (Krüger et al, 2018). Researches to obtain new α-amylase with better stability are often done by isolating extremophiles from various sources, such as hot spring (Sudan et al, 2018;Wu et al, 2018), deep sea (Jiang et al, 2015), and even honey (Du et al, 2018). Various studies have also been done to improve the stability of the enzyme through genetic engineering, immobilization, chemical modification and protein engineering (Dey et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

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Purification and Partial Characterization of α-Amylase Produced by a Thermo-Halophilic Bacterium Isolate PLS 75

2018

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Bio-based industries require stable enzymes in a broad range of environmental conditions. Extremophiles have attracted more interests as the source of such enzymes, one of which is α-amylase. This study aimed to purify and characterize α-amylase produced by a thermo-halophilic bacterium PLS 75 isolated from underwater fumaroles. Ammonium sulfate precipitation results showed that the highest specific α-amylase activity (21.7 U/mg) obtained at 40-60% saturation level, with a purity of 7.7-fold of the crude extract with 16.2% yield. Further purification using DEAE Sepharose column chromatography increased the enzyme purity 11.1-fold of the crude extract with 7.1% yield. Specific activity after column chromatography purification was 31.3 U/mg. The pure enzyme had a low molecular weight of 14 kDa. The enzyme showed the highest activity at 80 °C and pH 5. The activity increased to 126% when in methanol, while decreased when in ethyl acetate and chloroform. The characteristics of α-amylase with low molecular weight, which was active in acidic condition, stable in polar and non-polar solvents, may be used for for specific industrial needs.

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Section: Effect Of Temperature Ph and Organic Solventmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Purification and Partial Characterization of α-Amylase Produced by a Thermo-Halophilic Bacterium Isolate PLS 75

2018

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“…Thermostable amylolytic enzymes are one of the most interesting groups of enzymes for industrial processes, as they are important for the hydrolysis of starch at high temperatures, promoting the reactions and reducing the risk of contamination [66]. Several thermostable amylases have been reported from deep-sea microorganisms [51,52,67], some of which have been developed into products. For example, Fuelzyme ® , a product from Verenium Corporation (San Diego, CA, USA), utilises an alpha-amylase from the thermophile Thermococcus sp., which was isolated from a deep-sea hydrothermal vent.…”

Section: Deep-sea Thermophilic Enzymesmentioning

confidence: 99%

Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review

et al. 2019

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The deep sea, which is defined as sea water below a depth of 1000 m, is one of the largest biomes on the Earth, and is recognised as an extreme environment due to its range of challenging physical parameters, such as pressure, salinity, temperature, chemicals and metals (such as hydrogen sulphide, copper and arsenic). For surviving in such extreme conditions, deep-sea extremophilic microorganisms employ a variety of adaptive strategies, such as the production of extremozymes, which exhibit outstanding thermal or cold adaptability, salt tolerance and/or pressure tolerance. Owing to their great stability, deep-sea extremozymes have numerous potential applications in a wide range of industries, such as the agricultural, food, chemical, pharmaceutical and biotechnological sectors. This enormous economic potential combined with recent advances in sampling and molecular and omics technologies has led to the emergence of research regarding deep-sea extremozymes and their primary applications in recent decades. In the present review, we introduced recent advances in research regarding deep-sea extremophiles and the enzymes they produce and discussed their potential industrial applications, with special emphasis on thermophilic, psychrophilic, halophilic and piezophilic enzymes.Nearly three-quarters of the Earth's surface area is covered by ocean, the average depth of which is 3800 m, implying that the vast majority of our planet comprises deep-sea environments. The deep sea is one of the most mysterious and unexplored environments on the Earth, and it supports diverse microbial communities that play important roles in biogeochemical cycles [1]. The deep sea is also recognised as an extreme environment, as it is characterised by the absence of sunlight and the presence of predominantly low temperatures and high hydrostatic pressures, and these environmental conditions become even more challenging in particular habitats, such as deep-sea hydrothermal vents with their extremely high temperatures of >400 • C, deep hypersaline anoxic basins (DHABs) with their extremely high salinities and abysses of up to 11 km depth with their extremely high pressures.Deep-sea extremophiles are living organisms that can survive and proliferate in deep-sea environments that have extreme physical (pressure and temperature) and geochemical (pH, salinity and redox potential) conditions that are lethal to other organisms. The majority of deep-sea extremophiles belong to the prokaryotes, which are microorganisms in the domains of Archaea and Bacteria [2,3].These extremophilic microorganisms are functionally diverse and widely distributed in taxonomy [4], and they are classified into thermophiles (55 • C to 121 • C), psychrophiles (−2 • C to 20 • C), halophiles (2-5 M NaCl or KCl), piezophiles (>500 atmospheres), alkalophiles (pH > 8), acidophiles (pH < 4) and metalophiles (high concentrations of metals, e.g., copper, zinc, cadmium and arsenic) according to the extreme environments in which they grow and the extreme conditions they can tolerate. Ma...

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“…Efficient extracellular expression in Escherichia coli is nowadays possible due to different strategies with various signal peptide sequences. Several recent RSDA were expressed this way for example by using OmpA [51] or native signal peptide sequence [52]. We reported recently a new approach based on the fusion of recombinant precursor to the signal peptide of DsbA for overexpression and secretion of fully active α-amylase originated from Bacillus licheniformis ATCC 9945a (BliAmy) [53] by targeting recombinant precursors to the co-translational signal recognition-particle dependent pathway [54].…”

Section: Recent Advances In Rsda Upstream and Downstream Processingmentioning

confidence: 99%

Raw starch degrading α-amylases: an unsolved riddle

Božić

Lončar

Slavić

et al. 2017

Amylase

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Starch is an important food ingredient and a substrate for the production of many industrial products. Biological and industrial processes involve hydrolysis of raw starch, such as digestion by humans and animals, starch metabolism in plants, and industrial starch conversion for obtaining glucose, fructose and maltose syrup or bioethanol. Raw starch degrading α-amylases (RSDA) can directly degrade raw starch below the gelatinization temperature of starch. Knowledge of the structures and properties of starch and RSDA has increased significantly in recent years. Understanding the relationships between structural peculiarities and properties of RSDA is a prerequisite for efficient application in different aspects of human benefit from health to the industry. This review summarizes recent advances on RSDA research with emphasizes on representatives of glycoside hydrolase family GH13. Definite understanding of raw starch digesting ability is yet to come with accumulating structural and functional studies of RSDA.

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Characterization of a thermostable raw-starch hydrolyzing α-amylase from deep-sea thermophile Geobacillus sp.

Cited by 50 publications

References 25 publications

Purification and Partial Characterization of α-Amylase Produced by a Thermo-Halophilic Bacterium Isolate PLS 75

Purification and Partial Characterization of α-Amylase Produced by a Thermo-Halophilic Bacterium Isolate PLS 75

Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review

Raw starch degrading α-amylases: an unsolved riddle

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