Purification and biochemical characterization of a thermostable and acid-stable alpha-amylase from Bacillus licheniformis B4-423

Wu, Xiangrong; Wang, Yuxia; Tong, Bending; Xiang-hua, Chen; Chen, Jianhua

doi:10.1016/j.ijbiomac.2017.12.004

Cited by 86 publications

(51 citation statements)

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“…El rango de Tabla I. Efecto de la temperatura y pH sobre la actividad de las enzimas hidrolíticas del ciego del cuy (Cavia porcellus) (Effect of temperature and pH on the activity of hidrolytic enzymes of the cecal region of the cuy (Cavia porcellus) temperaturas óptimas para la producción de amilasas bacterianas aisladas de la industrialización de papas o de leche fresca ovina esta entre 35-80°C (Wind et al, 1994;;Konsoula et al, 2004). En cuanto al pH, no afectó la actividad amilolítica, es decir la actividad enzimática fue muy estable en el rango de pH evaluado, datos que concuerdan con un estudio reciente donde purificaron y caracterizaron bioquímicamente una amilasa de origen bacteriano aislada de fuentes termales (Xiangrong et al, 2017).…”

Section: Resultados Y Discusiónunclassified

Efecto de la Temperatura y pH sobre la Actividad de las Enzimas Hidrolíticas de la Región Cecal de Cuyes (Cavia porcellus)

et al. 2019

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El objetivo de este estudio fue evaluar el efecto de la temperatura y el pH sobre la actividad de las enzimas hidrolíticas de la región cecal de cuyes (Cavia porcellus). Este es el primer reporte sobre la actividad enzimática en el ciego de cuyes, evidenciando que existe actividad amilolítica, celulolítica, proteolítica y lipolítica. Los valores de las actividades evaluadas estuvieron en los siguiente rangos: actividad amilolítica (0.150 - 0.499 U/mg proteína), celulolítica (0.013 - 0.022 U/mg proteína), proteolítica (0.104 - 0.290 U/mg proteína) y lipolítica (2.227 - 4.049 U/mg proteína). Tanto en la actividad celulolítica, lipolítica y proteolítica hubo interacción entre temperatura y pH. La actividad amilolítica solo se vio afectada por la temperatura, evidenciándose mayor actividad enzimática a mayor temperatura (40°C). La actividad amilolítica es estable a cualquiera de los tres pH probados en este estudio. Además, la actividad amilolítica fue 10 veces más alta que la actividad celulolítica.

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Section: Resultados Y Discusiónunclassified

Efecto de la Temperatura y pH sobre la Actividad de las Enzimas Hidrolíticas de la Región Cecal de Cuyes (Cavia porcellus)

et al. 2019

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“…Purification of α-amylase is often done by a combination of several methods. The initial step was mostly done by salt precipitation, followed by chromatograpy methods (Wu et al, 2018;Du et al, 2018;Sudan et al, 2018). Of the five fractions after ammonium sulfate precipitation, Fraction 2 produced the highest activity (42.4 U/ mL) and protein concentration (2.09 mg/mL).…”

Section: Ammonium Sulfat Precipitationmentioning

confidence: 99%

“…The concentration of ammonium sulfate needed to produce optimum α-amylase specific activity varies. Precipitation of α-amylase is commonly carried out at concentrations of 60-80% (Al-Quadan et al, 2011;Sudan et al, 2018), although there is an α-amylase precipitated in only 30% concentration of salt (Wu et al, 2018). The surface of proteins from thermophilic bacteria contains plenty of charged residues.…”

Section: Ammonium Sulfat Precipitationmentioning

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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“…Bacillus licheniformis (BL) is a Gram (+) bacterium known for the synthesis of a wide range of medicinal, agricultural, pharmaceutical and industrial products. In the last years, it has been extensively used for largescale industrial production of exoenzymes, antibiotics and chemicals (Elshaghabee et al, 2017;Wu et al, 2018). BL strains are categorised by the World Health Organization as a GRAS organism (Generally Recognized As Safe), being active against many pathogens and free of toxins.…”

Section: Introductionmentioning

confidence: 99%

Carotenoid profile produced by Bacillus licheniformis Rt4M10 isolated from grapevines grown in high altitude and their antioxidant activity

Cohen

Dichiara

Jofré

et al. 2018

Int J of Food Sci Tech

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Summary Bacillus licheniformis (BL) strains are used for industrial production of exoenzymes, antibiotics and secondary metabolites, and also serve as probiotics. Some strains sequester heavy metals, promoting plant growth or inducing plant systemic resistance against stresses. However, investigations on the biological functions and applicability of carotenoids produced by BL had been less studied. In this study, the carotenoid profile produced by BL Rt4M10 was characterised during the accumulation period of culture and in response to diphenylamine (DPA), inhibitor of carotenoid biosynthesis. The antioxidant scavenging capacities of the carotenoid extracts against oxidative reactions inside the microbial cell and in vitro were also evaluated. Eighteen different carotenoids were analysed; their profile was modified along bacterial growth. DPA decreased carotenoid production by 70%, as well as the cells’ survival in hydrogen peroxide and the antioxidant capacity, thus demonstrating the role of carotenoids from Rt4M10 in oxidative stress.

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Purification and biochemical characterization of a thermostable and acid-stable alpha-amylase from Bacillus licheniformis B4-423

Cited by 86 publications

References 34 publications

Efecto de la Temperatura y pH sobre la Actividad de las Enzimas Hidrolíticas de la Región Cecal de Cuyes (Cavia porcellus)

Efecto de la Temperatura y pH sobre la Actividad de las Enzimas Hidrolíticas de la Región Cecal de Cuyes (Cavia porcellus)

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

Carotenoid profile produced by Bacillus licheniformis Rt4M10 isolated from grapevines grown in high altitude and their antioxidant activity

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