Purification and Characterization of Thermostable and Detergent-Stable Alpha-Amylase from Anoxybacillus sp. AH1

Acer, Ömer; Bekler, Fatma Matpan; Pirinççioğlu, Hemşe; Güven, Reyhan Gül; Güven, Kemal

doi:10.17113/ftb.54.01.16.4122

Cited by 22 publications

(10 citation statements)

References 36 publications

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“…Thermostable amylase from Anoxybacillus sp. AH1 also showed increased stability at 60 0 C within 120 mins [24].…”

Section: Discussionmentioning

confidence: 90%

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Isolation and characterization of alkaline amylase producers from the marine environment of Arabian sea coast

Pol¹,

Amin²

2022

GSC Biol. Pharm. Sci.

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Alkaline amylase producers were isolated from the marine environment of Arabian Sea coast. A total of 10 isolates were obtained from the soil and water samples collected from the marine environment. Five isolates namely; BCSS, JBWS, RBWS, BCWS and ALSS showed good growth on alkaline M9 media with 10% NaCl having starch as the primary carbon source. Based on their maximal amylase activity, three microbial cultures (BCSS, JBWS, and RBWS) were selected for the study. The crude enzyme from these purified cultures was extracted and partial characterization was carried out. The partial characterization study involved the effect of metal ions and surfactants and determination of optimal pH and temperature and its stability studies. The amylase activity was optimum for all three cultures at 60 0C whereas, the optimum pH was found to be pH 7, pH 8 and pH 9 for RBWS, JBWS and BCSS. The pH and temperature stability studies showed maximum amylase activity at its optimal conditions for 5h (300 mins) in the order BCSS>RBWS>JBWS. The amylase activity was found to increase with sodium (BCSS), manganese (RBWS) and potassium (JBWS) at 1:1 dilution. The cultures were stable with the surfactants (Tween -20, SDS and Triton-X) at 1:10 dilution of 1% surfactant and enzyme. BCSS was the most stable at high temperature and pH among all the isolates with an optimal amylase activity at pH 9 and temperature of 60 0C. The isolate was identified to be Bacillus nanhaiisediminis NH3. These remarkable properties indicated its great potential in industrial applications.

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“…Thermostable amylase from Anoxybacillus sp. AH1 also showed increased stability at 60 0 C within 120 mins [24].…”

Section: Discussionmentioning

confidence: 90%

“…A3-15 [26]. α-amylase isolated from Anoxybacillus sp.AH1 was significantly activated in presence of Mg +2 , Ca 2+ and inhibited with Zn 2+ and Cu 2+ [24]. Metal ions can activate the enzyme activity by stabilizing the structure of ES complex or sensitize the substrate to the attack of enzyme or take part in ion exchange process [32].…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of alkaline amylase producers from the marine environment of Arabian sea coast

Pol¹,

Amin²

2022

GSC Biol. Pharm. Sci.

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“…Inhibitory effect of EDTA (metal chelator) and Cd 2+ has been reported in previous studies [36,40]. Agüloglu et al [41] reported 79% inhibition (with 1 mM EDTA) and 87% inhibition (with 10 mM EDTA) on α-amylase from Anoxybacillus flavithermus, while Acer et al [42] reported 63% inhibition with 1 mM EDTA on αamylase from Anoxybacillus sp. AH1.…”

Section: Effect Of Chemical Agents On α-Amylase Activitymentioning

confidence: 81%

Production, Partial Purification and Characterization of Two α-Amylase Isoforms from Saccharomyces cerevisiae strain YOP 1/2-2 Isolated from Tchapalo (Côte d’Ivoire)

Ouattara

Thierry

Evrard

et al. 2020

JABB

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Amylases play an important role in biotechnology and find applications in several industrial fields such as pharmaceutical, food, paper, cosmetics and detergents. Thus, it appears necessary to identify new sources of amylase, especially from microbial origin, due to the low energy consumption, cost-effective, high metabolic diversity, rapid cell growth, non-toxic and eco-friendly characteristics. In the present report, we carried out the production and partial purification of α-amylase by Saccharomyces cerevisiae strains isolated from Tchapalo, a traditional alcoholic beverage of Côte d'Ivoire. Five fungal isolates were screened initially for α-amylase production by using method of wells on Yeast Extract Peptone Dextrose Agar medium, a complete medium for yeast growth. One step DEAE-Sepharose Fast Flow was achieved for partial purification of α-amylase obtained. Among yeasts, isolate S. cerevisiae YOP 1/2-2 was able to provoke starch hydrolysis halo of 15.067±0.12 mm on starch agar plate after 48 h of incubation at 30°C. The partial purification of resulting enzyme showed two protein peaks, designated α-amylase 1 (AMY1) and α-amylase 2 (AMY2) with amylolytic activity and specific activities of 1.57-1.58 U/mg protein. Both isoforms (AMY1 and AMY2) were thermostable with optimal activity at 50 and 55°C, respectively, and at pH ranged from 4.5 to 5.3 in 0.1 M sodium acetate buffer. EDTA and Cd2+ strongly inhibited α-amylase activity by 72-75% and 64-65%, respectively, whereas cations Ca2+ and Mn2+ showed 85-99% and 71% increased amylolytic activity, respectively. All these properties show the potential uses of α-amylases from S. cerevisiae in the industrial transformation of starch.

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“…When 10 mM EDTA was added to α-amylase from Anoxybacillus sp. AH1, the amylolytic activity dropped to 37%, with a 63% decrease in enzyme activity (Acer et al 2016).…”

Section: Metal Ions and Inhibitorsmentioning

confidence: 94%

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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Purification and Characterization of Thermostable and Detergent-Stable Alpha-Amylase from Anoxybacillus sp. AH1

Cited by 22 publications

References 36 publications

Isolation and characterization of alkaline amylase producers from the marine environment of Arabian sea coast

Isolation and characterization of alkaline amylase producers from the marine environment of Arabian sea coast

Production, Partial Purification and Characterization of Two α-Amylase Isoforms from Saccharomyces cerevisiae strain YOP 1/2-2 Isolated from Tchapalo (Côte d’Ivoire)

Purification and characterisation of thermostable α-amylases from microbial sources

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