Biosynthesis and industrial applications of α-amylase: a review

Farooq, Muhammad; Ali, Shaukat; Hassan, Ali; Tahir, Hafız Muhammad; Mumtaz, Shumaila; Mumtaz, Sadaf

doi:10.1007/s00203-020-02128-y

Cited by 71 publications

(36 citation statements)

References 44 publications

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“…The activity of α-amylase was determined by the dinitrosalicylic acid solution (DNS) method [24,25]. To prepare the DNS reagent, 10.6 g 3,5-dinitrosalicylic acid was dissolved in 500 mL distilled water in oil bath at 48 • C, then 19.8 g sodium hydroxide solution was added slowly with stirring.…”

Section: Activity Of α-Amylasementioning

confidence: 99%

Self-Encapsulation of Biomacromolecule Drugs in Porous Microscaffolds with Aqueous Two-Phase Systems

Kang

Cai

et al. 2021

Pharmaceutics

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At present, the most commonly used methods of microencapsulation of protein drugs such as spray drying, multiple emulsification, and phase separation, can easily cause the problem of protein instability, which leads to low bioavailability and uncontrolled release of protein drugs. Herein, a novel method to encapsulate protein drugs into porous microscaffolds effectively and stably was described. Ammonium hydrogen carbonate (NH4HCO3) was employed to prepare porous microscaffolds. α-Amylase was encapsulated into the porous microscaffolds without denaturing conditions by an aqueous two-phase system (PEG/Sulfate). The pores were closed by heating above the glass transition temperature to achieve a sustained release of microscaffolds. The pore-closed microscaffolds were characterized and released in vitro. The integrity and activity of protein drugs were investigated to verify that this method was friendly to protein drugs. Results showed that the pores were successfully closed and a high loading amount of 9.67 ± 6.28% (w/w) was achieved. The pore-closed microscaffolds released more than two weeks without initial burst, and a high relative activity (92% compared with native one) of protein demonstrated the feasibility of this method for protein drug encapsulation and delivery.

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Section: Activity Of α-Amylasementioning

confidence: 99%

Self-Encapsulation of Biomacromolecule Drugs in Porous Microscaffolds with Aqueous Two-Phase Systems

Kang

Cai

et al. 2021

Pharmaceutics

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“…The effect of metal ions on BvAmylase was tested by measuring the activity in the presence of metal ions. The results showed that all of the metal ions tested (Mn 2+ , Zn 2+ , Fe 2+ , Na + , Ca 2+ , K + , Mg 2+ , Cu 2+ ) inhibited the enzymatic activity of BvAmylase at both 2 mM and 5 mM except Co 2+ which promoted the enzymatic activity at 2 mM and inhibited the The purified BvAmylase was preincubated in varying pH (3)(4)(5)(6)(7)(8)(9) in the respective buffer for 48 h, and the residual enzyme activity was tested by the DNS method. The highest activity and the highest residual activity were taken as the control (100%).…”

Section: Effect Of Ph On the α-Amylase Activity And Stabilitymentioning

confidence: 99%

“…Alpha-amylase was first commercialized in 1984 as a drug adjuvant for the treatment of digestive disorders. Now, α-amylase has been widely used in food, detergent, beer brewing, textile, alcohol, and paper industries [7]. In addition, α-amylase is used in pharmaceutical, biofuel production, and environmental remediation [7,8].…”

Section: Introductionmentioning

confidence: 99%

“…Now, α-amylase has been widely used in food, detergent, beer brewing, textile, alcohol, and paper industries [7]. In addition, α-amylase is used in pharmaceutical, biofuel production, and environmental remediation [7,8]. The increasing demand in various industries requires enzymes with suitable characteristics, therefore, the discovery of new α-amylases and improvement of the existing ones are of interest.…”

Section: Introductionmentioning

confidence: 99%

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Bacillus velezensis Identification and Recombinant Expression, Purification, and Characterization of Its Alpha-Amylase

Zhang

Chen

et al. 2021

Fermentation

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Amylases account for about 30% of the global market of industrial enzymes, and the current amylases cannot fully meet industrial needs. This study aimed to identify a high α-amylase producing bacterium WangLB, to clone its α-amylase coding gene, and to characterize the α-amylase. Results showed that WangLB belonged to Bacillus velezensis whose α-amylase gene was 1980 bp coding 659 amino acids designated as BvAmylase. BvAmylase was a hydrophilic stable protein with a signal peptide and a theoretical pI of 5.49. The relative molecular weight of BvAmylase was 72.35 kDa, and was verified by SDS-PAGE. Its modeled structure displayed that it was a monomer composed of three domains. Its optimum temperature and pH were 70 °C and pH 6.0, respectively. It also showed high activity in a wide range of temperatures (40–75 °C) and a relatively narrow pH (5.0–7.0). It was a Ca2+-independent enzyme, whose α-amylase activity was increased by Co2+, Tween 20, and Triton X-100, and severely decreased by SDS. The Km and the Vmax of BvAmylase were 3.43 ± 0.53 and 434.19 ± 28.57 U/mg. In conclusion, the α-amylase producing bacterium WangLB was identified, and one of its α-amylases was characterized, which will be a candidate enzyme for industrial applications.

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“…α-Amylase (EC 3.2.1.1) capable of hydrolyzing α-1,4-glycosidic bonds in starch and related polymers into glucose, maltose, and maltotriose units. Therefore, α-amylases have a wide range of industrial applications in food processing, beverage, pharmaceutical, biofuels, detergent, and textile industries [5][6]. Various αamylases are widely distributed in animals, plants, and microorganisms.…”

Section: Introductionmentioning

confidence: 99%

High-Throughput Screening of Higher Α-Amylase Producing Bacillus Licheniformis by Fluorescence-Activated Droplet Sorting

Yuan

Tong

et al. 2021

Preprint

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Backgroundα-Amylases is one of the most important starch degrading enzymes and has the widest range of industrial applications. Bacillus licheniformis has been widely used as a cell factory for industrial production of amylase. However, difficulties in genetic modification of B. licheniformis have limited its widespread use. Directed evolution, based on the combination of random mutagenesis and high throughput screening (HTS), has been proven an effective strategy in strain improvement for increasing the productivity, but it requires a suitable HTS system to screen the desired mutants. Droplet-based microfluidics has emerged as a powerful tool for single-cell screening with ultra-high throughput, however, the accessibility of a droplet microfluidic HTS platform to users having no background in microfluidics is still an issue. ResultsHere, we first developed a microfluidic HTS platform based on fluorescence-activated droplet sorting (FADS) technology. This platform allowed (i) encapsulation of single cells in monodisperse water-in-oil droplets; (ii) cell growth and protein production in droplets; (iii) sorting of droplets based on their fluorescence intensities. To validate the platform, a model selection experiment of a binary mixture of Bacillus strains was performed and a 45.6-fold enrichment was achieved at a sorting rate of 300 droplets per second. Furthermore, we used the platform for the selection of higher α-amylase-producing strains from a library of B. licheniformis strains (a strain already used at industrial-scale). The B. licheniformis mutant library was generated by atmospheric and room temperature plasma (ARTP) mutagenesis. The clones displaying over 50% improvement in α-amylases productivity compared to the wild-type were isolated.ConclusionsWe established an efficient droplet microfluidic platform which consisted of droplet generation, droplet incubation, and sorting of droplets with a throughput of up to 1 × 106 droplets per h. The screening platform was demonstrated by successfully identifying B. licheniformis clones with improved α-amylase production. We believe that the droplet platform could be extended to the development of other industrially valuable strains.

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Biosynthesis and industrial applications of α-amylase: a review

Cited by 71 publications

References 44 publications

Self-Encapsulation of Biomacromolecule Drugs in Porous Microscaffolds with Aqueous Two-Phase Systems

Self-Encapsulation of Biomacromolecule Drugs in Porous Microscaffolds with Aqueous Two-Phase Systems

Bacillus velezensis Identification and Recombinant Expression, Purification, and Characterization of Its Alpha-Amylase

High-Throughput Screening of Higher Α-Amylase Producing Bacillus Licheniformis by Fluorescence-Activated Droplet Sorting

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