Microbial α-amylases: a biotechnological perspective

Gupta, Rani; Gigras, Paresh; Mohapatra, Harapriya; Goswami, Vineet Kumar; Chauhan, Bhavna

doi:10.1016/s0032-9592(03)00053-0

Cited by 1,130 publications

(832 citation statements)

References 132 publications

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“…Although amylases originate from different sources (animals, plants and microorganisms), microbial amylases generally meet industrial demands best, due to their short growth period and productivity (6). Its extensive application in food, starch liquefaction, saccharification, detergent, brewing, paper, textile and distilling industries, has led to a greater stress for the increase in the indigenous production of α-amylase (12). With the advent of new frontiers in biotechnology, the spectrum of amylase application has expanded into many other fields, such as clinical, medical and analytical chemistry.…”

Section: Introductionmentioning

confidence: 99%

Comparative study on production of α-Amylase from Bacillus licheniformis strains

Divakaran¹,

Chandran²,

Chandran³

2011

Braz. J. Microbiol.

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Alpha amylase (α-1, 4-glucan-glucanhydrolase, EC 3.2.1.1), an extracellular enzyme, degrades α, 1-4 glucosidic linkages of starch and related substrates in an endo-fashion producing oligosaccharides including maltose, glucose and alpha limit dextrin (7). The present study deals with the production and comparative study of production of α-amylase from two strains of Bacillus licheniformis, MTCC 2617 and 2618, by using four different substrates, starch, rice, wheat and ragi powder as carbon source by submerged fermentation. The effect of varying pH and incubation temperature, activator, inhibitor, and substrate concentration was investigated on the activity of α-amylase produced by MTCC strain 2618. The results shows that the production of the α-amylase by the B.licheniformis strain MTCC 2618, using four different substrates were found to be maximum (Starch 3.64 IU/ml/minutes, Rice powder 2.93 IU/ml/minutes, Wheat powder 2.67 IU/ml/minutes, Ragi powder 2.36 IU/ml/minutes) on comparing the enzyme production of two strains. It was also observed that the maximum production was found on the 3 rd day (i.e. 72 hr) and characterization of crude enzyme revealed that optimum activity was at pH 7 and 37°C.

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Section: Introductionmentioning

confidence: 99%

Comparative study on production of α-Amylase from Bacillus licheniformis strains

Divakaran¹,

Chandran²,

Chandran³

2011

Braz. J. Microbiol.

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“…According to Gupta et al (2003), organic nitrogen sources are preferred for the production of α-amylase by bacteria. On the other hand, various inorganic salts, such as ammonium sulfate, sodium nitrate and ammonium nitrate, have been reported in improved yields of α-amylase by fungi.…”

Section: Resultsmentioning

confidence: 99%

“…According to Gupta et al (2003), amylases are divided into two groups, the endo-amylases and exo-amylases. Endo-amylases catalyze hydrolyses within the starch molecule in various points of the chain simultaneously.…”

Section: Introductionmentioning

confidence: 99%

Characterization of -amylase produced by the endophytic strain of Penicillium digitatum in solid state fermentation (SSF) and submerged fermentation (SMF)

Onofre¹,

Abatti²,

Refosco³

et al. 2016

Afr. J. Biotechnol.

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α-Amylases are enzymes responsible for breaking the α-1,4 bond in polysaccharides with three or more glucose units, occupying the second place in the most widely employed enzymes in industry in the world. The objective of this study was to compare the yields of α-amylase produced by the endophytic fungus, Penicillium digitatum, strain D1-FB, isolated from Baccharis dracunculifolia D.C. (Asteraceae), through the solid state fermentation (SSM) and submerged fermentation (SmF) processes, in addition to characterizing the produced enzyme. The two fermentations were conducted for 120 h, taking samples every 24 h to obtain the peaks of production. The enzymes were characterized according to their optimal pH and temperature for performance and stability regarding the incubation in the presence of ions, variations in pH and temperature. The maximum yield of the enzyme was observed with SSF, using rice bran as substrate after 72 h of fermentation, with 1,625 U/mL. The α-amylase had an optimal pH at 6.5 and optimal temperature at 37°C. All the ions resulted in a decrease in the activity of α-amylase in the concentration of 5 mM. The enzyme proved to be quite stable in a pH range of 6.0 to 7.5 and up to the temperature of 37°C, but it presented great drops in activity with temperatures above 45°C and in the presence of ions at the concentration of 5 mM.

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“…This causes the formation of linear and branched oligosaccharides of various chain lengths. Exoamylases hydrolyze from the nonreducting end, successively resulting in short end products (Gupta, et al, 2003). Fig.…”

Section: Selection Of the Starchmentioning

confidence: 99%