Characterization and stability studies on surfactant, detergent and oxidant stable α-amylase from marine haloalkaliphilic Saccharopolyspora sp. A9

Chakraborty, Samrat; Khopade, Abhijeet; Ren, Biao; Wang, Jian; Li, Xiangyang; Mahadik, Kakasaheb R.; Chopade, Balu A.; Zhang, Lixin; Kokare, Chandrakant

doi:10.1016/j.molcatb.2010.09.009

Cited by 103 publications

(54 citation statements)

References 32 publications

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“…Enzyme activity had slightly decreased in the case of Triton X-100 retaining 63 % relative activity with concentration of 2 %. These findings indicated that the enzyme was highly stable in the presence of surfactants and oxidizing agents which was supported by various reports 47,[51][52][53] . The stability of enzyme towards surfactants and oxidizing agents revealed its potential utilization in detergent industries.…”

Section: Effect Of Surfactants and Oxidizing Agentsupporting

confidence: 84%

Study on Some Properties of Calcium-dependent a -Amylase from Bacillus subtilis through Submerged Fermentation of Wheat Bran

Irfan¹

2017

Chem.Biochem.Eng.Q.

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University of the Punjab new campus Lahore PakistanThis study reveals the production of α-amylase through Bacillus subtilis by submerged fermentation of wheat bran as a substrate. Various conditions were optimized and maximum production was observed at initial medium pH of 7.0, incubation temperature of 35 °C with agitation speed of 140 rpm for 48 h of fermentation period. Peptone, ammonium sulphate and soluble starch favored enzyme production as nitrogen and carbon source, respectively. The crude α-amylase was purified 2.03-fold by column (sephadex G-100) chromatography having specific activity of 480.0 U mg -1 . The purified enzyme had molecular mass of 54.18 kDa as determined by 12 % SDS-PAGE. The optimum pH and temperature of the enzyme was 8.5 and 60 °C, respectively. Ca 2+ played an important role in the stability of the enzyme retaining relative activity of 87 % and 67 % at pH 9.5 and 80 °C, revealing the Ca 2+ dependency respectively. The enzyme was highly stable towards surfactants and oxidizing agents. Kinetic study indicated that the enzyme exhibit K m and V max value of 4.4 mg mL -1 and 714.2 U mL -1 using soluble starch as a substrate respectively.

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Section: Effect Of Surfactants and Oxidizing Agentsupporting

confidence: 84%

Study on Some Properties of Calcium-dependent a -Amylase from Bacillus subtilis through Submerged Fermentation of Wheat Bran

Irfan¹

2017

Chem.Biochem.Eng.Q.

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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%

“…A3-15 Compost soil Starch agar Arikan [18] Saccharopolyspora sp. A9 Marine sediment Starch agar Chakraborty et al [25] Bacillus licheniformis AS08E Soil Starch agar Roy and Mukherjee [24] Streptomyces strain A3 Marine sediment Starch agar Chakraborty et al [26] Bacillus subtilis AS-SO1a Soil Starch agar Roy et al [9] Alicyclobacillus acidocaldarius Water effluent Starch agar Satheeshkumar et al [27] Bacillus sp. strain TSCVKK Soil Starch agar Kiran and Chandra [21] Nesterenkonia sp.…”

Section: Microorganismmentioning

confidence: 99%

“…[25], and Streptomyces sp. [26] are also used for detergentcompatible amylases production ( Table 2). Submerged fermentation (SmF) [9, 18-22; 26-29] and solid state fermentation (SSF) [24,29] are used for the production of bacterial detergent amylases.…”

Section: Production Of Bacterial Detergent-compatible Amylasesmentioning

confidence: 99%

“…Starch is often used as a carbon source for detergent-compatible amylase production by bacteria [9, 18-20, 22, 25, 27, 28]. Other carbohydrates like maltose [26] and dextrin [21] were also used as carbon sources. Glycerol was also the best carbon source for amylase production by Bacillus cereus GA6 [23].…”

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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Marine Microbial Enzymes: Biotechnological and Biomedical Aspects

Sana

2013

Marine Microbiology

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Characterization and stability studies on surfactant, detergent and oxidant stable α-amylase from marine haloalkaliphilic Saccharopolyspora sp. A9

Cited by 103 publications

References 32 publications

Study on Some Properties of Calcium-dependent a -Amylase from Bacillus subtilis through Submerged Fermentation of Wheat Bran

Study on Some Properties of Calcium-dependent a -Amylase from Bacillus subtilis through Submerged Fermentation of Wheat Bran

Detergent-Compatible Bacterial Amylases

Marine Microbial Enzymes: Biotechnological and Biomedical Aspects

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