Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain

Baltaş, Nimet; Dinçer, Barbaros; Ekinci, Arife Pınar; Kolaylı, Sevgi; Adıgüzel, Ahmet

doi:10.1590/1678-4324-2016160346

Cited by 23 publications

(12 citation statements)

References 31 publications

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“…After the precipitation of salt was suspended in MOPS buffer, the enzyme solution was washed and subjected to an Amicon ultrafiltration membrane with the MWCO of 30 kDa. A 75.2% yield recovery as well as 4.4-fold purification were reported with this ultrafiltration technique after performing salt precipitation (Baltas et al 2016). Similarly, after performing salt precipitation, enzyme solution containing α-amylase expressed in Talaromyces pinophilus 1-95 was concentrated using a 10-kDa MWCO ultra-filtration membrane with 80.13% yield recovery and 1.77fold purification being reported (Xian et al 2015).…”

Section: Ultrafiltrationmentioning

confidence: 87%

“…An example of ultrafiltration after ammonium sulfate precipitation was performed by Baltas et al (2016). The work involved purifying α-amylase expressed in a thermophilic Anoxybacillus thermarum A4 strain.…”

Section: Ultrafiltrationmentioning

confidence: 99%

“…Referring to Table 6, the most frequently equipped SEC matrix is Sephadex G-100 (Chen et al 2015;Baltas et al 2016;Allala et al 2019;El-Sayed et al 2019). This matrix shown promising yields while purifying α-amylases produced by Anoxybacillus thermarum A4 strain (74.6%), Bacillus subtilis WB800 (41.7%), Escherichia coli BL21 (76.53%), and Tepidimonas fonticaldi strain HB23 (41%).…”

Section: Size-exclusion Chromatographymentioning

confidence: 99%

“…However, both fungal thermostable α-amylases expressed in Aspergillus flavus NSH9 (Karim et al 2018) and Trichoderma pseudokoningii (Abdulaal 2018) exhibited the lowest optimum temperature at 50 ˚C, while α-amylase produced by Komagataella phaffii (Wang et al 2015) showed the highest optimum temperature at 90 °C. Bacterial α-amylases have a wide range of optimum pH from pH 5.0 (Wu et al 2017;Emtenani et al 2015) to 10.5 (Baltas et al 2016), while fungal α-amylases were shown to have their optimum pH ranging from pH 5.0 (Karim et al 2018;Sethi et al 2016b;Xian et al 2015) to pH 9.0 (Ali et al 2014).…”

Section: Optimum Temperature and Phmentioning

confidence: 99%

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Purification and characterisation of thermostable α-amylases from microbial sources

Lim

Oslan

2019

BioRes

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α-Amylases (E.C 3.2.1.1) hydrolyse starch into smaller moieties such as maltose and glucose by breaking α-1,4-glycosidic linkages. The application of α-amylases in various industries has made the large-scale productions of these enzymes crucial. Thermostable α-amylase that catalyses starch degradation at the temperatures higher than 50 °C is favourable in harsh industrial applications. Due to ease in genetic manipulation and bulk production, this enzyme is most preferably produced by microorganisms. Bacillus sp. and Escherichia coli are commonly used microbial expression hosts for α-amylases (30 to 205 kDa in molecular weight). These amylases can be purified using ultrafiltration, salt precipitation, dialysis, and column chromatography. Recently, affinity column chromatography has shown the most promising result where the recovery rate was 38 to 60% and purification up to 13.2-fold. Microbial thermostable α-amylases have the optimum temperature and pH ranging from 50 °C to 100 °C and 5.0 to 10.5, respectively. These enzymes have high specificity towards potato starch, wheat starch, amylose, and amylopectin. EDTA (1 mM) gave the highest inhibitory effect (79%), but Ca2+ (5 mM) was the most effective co-factor with 155%. This review provides insight regarding thermostable α-amylases obtained from microbial sources for industrial applications.

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Section: Ultrafiltrationmentioning

confidence: 87%

Section: Ultrafiltrationmentioning

confidence: 99%

Section: Size-exclusion Chromatographymentioning

confidence: 99%

Section: Optimum Temperature and Phmentioning

confidence: 99%

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Purification and characterisation of thermostable α-amylases from microbial sources

Lim

Oslan

2019

BioRes

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“…Potential applications for some of Anoxybacillus species were reported previously, particularly for the production of bioactive molecules and biocatalysts that may be significant for industrial processes. Anoxybacillus species were found to be very efficient in producing different enzymes like lipase , xylanase , and amylase by using different substrates. Finore et al .…”

Section: Discussionmentioning

confidence: 99%

Isolation of thermophilic Anoxybacillus beppuensis JF84 and production of thermostable amylase utilizing agro–dairy wastes

Jabeen

Hussain

Manzoor

et al. 2018

Env Prog and Sustain Energy

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Extremophiles are the organisms that can be manipulated for various industrial activities. Agro–dairy wastes are being utilized for economical production of enzymes employing microbes. In this regard, thermophilic amylolytic bacterium was isolated from soil in vicinity of hot spring near Chakwal, Pakistan. The isolated bacterium was rod‐shaped, positive for Gram staining, and endospores former. The isolate was able to utilize sugars like, maltose, xylose, fructose, sachorose, sorbitol, mannose, mannitol, arabinose and polysaccharides like gelatin and starch. The isolate grew over a wide temperature range (40–70°C) and pH (4–9). It exhibited enough growth with different nitrogen sources which could produce amylase up to 0.72 U/mL, while hydrolyzing starch. Phylogenetic analysis based on 16S rRNA gene sequence showed that it belongs to Anoxybacillus beppuensis under Accession number KF254912 (JF84). The DNA G+C content were 56.59%. The isolate JF84 showed fourfold purification and percentage yield was estimated to be 94.21% as compared to crude enzyme. The decreasing order of substrate suitability for amylase production was found to be sugarcane bagasse (SCB) > wheat straw (WS) > sugarcane bagasse and whey (SB + W) > whey (W). A. beppuensis JF84 yielded enough thermostable α‐amylase in economical substrates as well as tolerated broad pH and temperature suggesting its wide economical commercial use in amylase‐dependent industries. © 2018 American Institute of Chemical Engineers Environ Prog, 38: 417–423, 2019

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Geobacillus and Anoxybacillus spp. from Terrestrial Geothermal Springs Worldwide: Diversity and Biotechnological Applications

Margaryan

Shahinyan

Hovhannisyan

et al. 2018

Extremophiles in Eurasian Ecosystems: Ecology, Diversity, and Applications

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Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain

Abstract: ABSTRACT

Cited by 23 publications

References 31 publications

Purification and characterisation of thermostable α-amylases from microbial sources

Purification and characterisation of thermostable α-amylases from microbial sources

Isolation of thermophilic Anoxybacillus beppuensis JF84 and production of thermostable amylase utilizing agro–dairy wastes

Geobacillus and Anoxybacillus spp. from Terrestrial Geothermal Springs Worldwide: Diversity and Biotechnological Applications

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