Purification and characterization of highly thermostable α-amylase from thermophilic Alicyclobacillus acidocaldarius

Kumar, Gudi Satheesh; Chandra, M. Subhosh; Mallaiah, K. V.; Sreenivasulu, P.; Choi, Yong-Lark

doi:10.1007/s12257-009-0072-5

Cited by 27 publications

(25 citation statements)

References 26 publications

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“…Some other bacteria are isolated from the marine sediment [25,26], watery environment [27,28], or fermented food [29] (Table 1). They are screened from the soil sample by serial dilution and Table 1 Isolation and screening of detergent-compatible amylase-producing bacteria…”

Section: Screening Of Detergent Amylase-producing Bacteriamentioning

confidence: 99%

“…strain TSCVKK Soil Starch agar Kiran and Chandra [21] Nesterenkonia sp. strain F Lake water Starch agar Shafiei et al [28] Bacillus cohnii US147 Soil Starch agar Ghorbel et al [22] Bacillus subtilis DM-03 Fermented food Starch agar Mukherjee et al [29] spread plating on the starch agar plate. The formation of clear zone around the organism is an indication of amylolytic activity.…”

Section: Microorganismmentioning

confidence: 99%

“…Some carbon sources like potato peel are cheap, and thus the cost of the fermentation is not high [29] ( Table 2). Starch of 1 % strength is generally used for bacterial detergent amylase production [18,22,27,28]. Soluble starch and its hydrolytic product were mostly reported to be best inducers of α-amylases [30].…”

Section: Production Of Bacterial Detergent-compatible Amylasesmentioning

confidence: 99%

“…The inoculum size plays an important role in microbial growth and thus in detergent amylase production. The inoculum size in the 0.5-2 % range led to an optimum detergent amylase production by bacteria [20,23,25,26,28]. A high inoculum level is usually inhibitory due to limitation of nutrient supply in the production medium leading to poor growth, resulting in fewer yields.…”

Section: Production Of Bacterial Detergent-compatible Amylasesmentioning

confidence: 99%

“…This was ascribed to the disruption of transport mechanisms across the microbial membrane that prevents the liberation of the enzyme [34]. Most of the bacterial detergent-compatible amylases are produced in the temperature range of 20-60°C [18][19][20][21][22][23][24][25][26][27][28][29] ( Table 2). The amylase of B. subtilis AS-SO1a was maximally produced in the 15-55°C range [9].…”

Section: Production Of Bacterial Detergent-compatible Amylasesmentioning

confidence: 99%

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Detergent-Compatible Bacterial Amylases

Niyonzima

2014

Appl Biochem Biotechnol

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Proteases, lipases, amylases, and cellulases are enzymes used in detergent formulation to improve the detergency. The amylases are specifically supplemented to the detergent to digest starchy stains. Most of the solid and liquid detergents that are currently manufactured contain alkaline enzymes. The advantages of using alkaline enzymes in the detergent formulation are that they aid in removing tough stains and the process is environmentally friendly since they reduce the use of toxic detergent ingredients. Amylases active at low temperature are preferred as the energy consumption gets reduced, and the whole process becomes cost-effective. Most microbial alkaline amylases are used as detergent ingredients. Various reviews report on the production, purification, characterization, and application of amylases in different industry sectors, but there is no specific review on bacterial or fungal alkaline amylases or detergent-compatible amylases. In this mini-review, an overview on the production and property studies of the detergent bacterial amylases is given, and the stability and compatibility of the alkaline bacterial amylases in the presence of the detergents and the detergent components are highlighted.

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Section: Screening Of Detergent Amylase-producing Bacteriamentioning

confidence: 99%

Section: Microorganismmentioning

confidence: 99%

Section: Production Of Bacterial Detergent-compatible Amylasesmentioning

confidence: 99%

Section: Production Of Bacterial Detergent-compatible Amylasesmentioning

confidence: 99%

Section: Production Of Bacterial Detergent-compatible Amylasesmentioning

confidence: 99%

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Detergent-Compatible Bacterial Amylases

Niyonzima

2014

Appl Biochem Biotechnol

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Thermostable α‐amylase immobilization: Enhanced stability and performance for starch biocatalysis

Kumar

Rather

Gurramkonda

et al. 2015

Biotech and App Biochem

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The uses of thermostable starch hydrolytic biocatalysts are steadily increasing for the industrial application because of their obvious need for biocatalytic performance at elevated temperatures. The starch liquefaction and saccharification can be carried out simultaneously by the use of thermostable starch hydrolytic biocatalysts, thus minimizing the unit operations, time, and efforts. The cost factor hampers the industrialization of expensive soluble (free) enzymes for biocatalytic applications and the immobilization of enzymes offers promising alternative to the hurdle. The present investigation was aimed for immobilization of thermostable α-amylase using calcium alginate, and statistical optimization studies were carried out for enhanced biocatalytic performance. Initially, one-parameter at a time optimization studies were carried out for identification of significant factors influencing the immobilization. Furthermore, a statistical approach, response surface methodology, was applied for immobilization of α-amylase. The immobilized α-amylase in alginate microbeads showed enhanced stability to temperature and reusable property for up to seven cycles (with the retention of 50% initial activity). Finally, the kinetic behavior of free and immobilized enzyme showed the Km value of 1.2% and 2.6% (w/v) and Vmax of 1,020 and 1,030 U, respectively. Fifty percent reduction in affinity of the immobilized enzyme toward substrate was compensated by its longer stability.

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Characterization of an acidophilic and thermostable α‐amylase from Alicyclobacillus sendaiensis NUST

Sheng

Yang

et al. 2012

Starch Stärke

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This paper describes the characterization of an acidophilic and thermostable α‐amylase from Alicyclobacillus sendaiensis NUST. The MW of this enzyme was estimated to be 56 kDa by SDS–PAGE. The enzyme was stable over a range of pH from 2.5 to 5.5 with an optimum around 3.5. Maximum activity of the α‐amylase was observed at pH 3.5 and 85°C in the presence of soluble starch as substrate. The enzyme activity was decreased by Mg2+, Cu2+, Zn2+, Al3+, K+, Li+, Ag+, urea, EDTA, trichloroacetic acid and Tween 60 and inhibited by Hg2+, Ce2+ and SDS, whereas the activity was increased by Mn2+, DTT, and β‐mercaptoethanol. Ca2+and Fe2+ did not affect the enzyme activity.

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Purification and characterization of highly thermostable α-amylase from thermophilic Alicyclobacillus acidocaldarius

Cited by 27 publications

References 26 publications

Detergent-Compatible Bacterial Amylases

Detergent-Compatible Bacterial Amylases

Thermostable α‐amylase immobilization: Enhanced stability and performance for starch biocatalysis

Characterization of an acidophilic and thermostable α‐amylase from Alicyclobacillus sendaiensis NUST

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