Aspects and Recent Trends in Microbial α-Amylase: a Review

Paul, Jai Shankar; Gupta, Nisha; Beliya, Esmil; Tiwari, Sakshi; Jadhav, S. K.

doi:10.1007/s12010-021-03546-4

Cited by 63 publications

(39 citation statements)

References 188 publications

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“…However, α-amylase from WangLB, B. subtilis JS-200449, and Bacillus subtilis showed the optimal activity at pH 9.0, pH 8.0, and pH 7.0, respectively [11,26,39]. In the literature, the optimal pH of α-amylase from Bacillus was even ranged from 4.5 to 10.5 [14,40].…”

Section: Discussionmentioning

confidence: 97%

“…There were three Ca 2+ binding sites N142, D187, and D212 near the barrel (Figure 6B). The binding of Ca 2+ can stabilize the structure of the enzyme [14]. B was a long loop that protrudes the surface, and domain C was composed of eight antiparallel beta-sheet structures (Figure 6A).…”

Section: Cloning Sequence Analysis Of the Bvamylase Gene And Construction Of The Prokaryotic Expression Plasmidmentioning

confidence: 99%

“…There were three Ca 2+ binding sites N142, D187, and D212 near the barrel (Figure 6B). The binding of Ca 2+ can stabilize the structure of the enzyme [14].…”

Section: Cloning Sequence Analysis Of the Bvamylase Gene And Construction Of The Prokaryotic Expression Plasmidmentioning

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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Section: Discussionmentioning

confidence: 97%

Section: Cloning Sequence Analysis Of the Bvamylase Gene And Construction Of The Prokaryotic Expression Plasmidmentioning

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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“…are extensively used in several industries. For instance, food, brewery, syrups, textile, detergent, pulp, paper, pharmaceutical, environmental, biofuel, healthcare, clinical, and analytical chemistry industries, among others [ 1 , 3 , 4 ]. Nowadays, α-amylases hold the major world market share of enzymes, accounting for approximately 25–30% of the world´s enzyme production [ 2 , 3 ].…”

Section: Introductionmentioning

confidence: 99%

“…α-Amylases catalyze the hydrolysis of starch by cleaving the internal α-1,4-glycosidic linkages to produce limit dextrin, short-chain oligosaccharides, maltotriose, maltose, and glucose [ 3 ]. Although α-amylases can be obtained from several sources, such as animals, plants, and microorganisms, most industrial applications use microbial α-amylases, mainly from bacteria and filamentous fungi [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Production of extracellular α-amylase by single-stage steady-state continuous cultures of Candida wangnamkhiaoensis in an airlift bioreactor

et al. 2022

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The kinetics of growth and α-amylase production of a novel Candida wangnamkhiaoensis yeast strain were studied in single-stage steady-state continuous cultures. This was performed in a split-cylinder internal-loop airlift bioreactor, using a variety of carbon sources as fermentation substrates. Results showed that the steady-state yields of cell mass from carbohydrates were practically constant for the range of dilution rates assayed, equaling 0.535 ± 0.030, 0.456 ± 0.033, and 0.491 ± 0.035 g biomass/g carbohydrate, when glucose, maltose, and starch, respectively were used as carbon sources. No α-amylase activity was detected when glucose was used as the carbon source in the influent medium, indicating that α-amylase synthesis of C. wangnamkhiaoensis is catabolically repressed by glucose. Contrastingly, maltose and starch induce synthesis of α-amylase in C. wangnamkhiaoensis, with starch being the best α-amylase inducer. The highest α-amylase volumetric and specific activities (58400 ± 800 U/L and 16900 ± 200 U/g biomass, respectively), and productivities (14000 ± 200 U/L·h and 4050 ± 60 U/g biomass·h, respectively) were achieved at a dilution rate of 0.24 h-1 using starch as the carbon source. In conclusion, single-stage steady-state continuous culture in an airlift bioreactor represents a powerful tool, both for studying the regulatory mechanisms of α-amylase synthesis by C. wangnamkhiaoensis and for α-amylase production. Furthermore, results showed that C. wangnamkhiaoensis represents a potential yeast species for the biotechnological production of α-amylase, which can be used for the saccharification of starch. This offers an attractive renewable resource for the production of biofuels (particularly bioethanol), representing an alternative to fossil fuels with reduced cost of substrates.

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Exploration of computational approaches to predict the structural features and recent trends in α‐amylase production for industrial applications

Shad

Hussain

Usman

et al. 2023

Biotech & Bioengineering

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Amylases are biologically active enzymes that can hydrolyze starch to produce dextrin, glucose, maltose, and oligosaccharides. The amylases contribute approximately 30% to the global industrial enzyme market. The globally produced amylases are widely used in textile, biofuel, starch processing, food, bioremediation of environmental pollutants, pulp, and paper, clinical, and fermentation industries. The purpose of this review article is to summarize recent trends and aspects of α-amylases, classification, microbial production sources, biosynthesis and production methods, and its broad-spectrum applications for industrial purposes, which will depict the latest trends in α-amylases production. In the present article, we have comprehensively compared the biodiversity of α-amylases in different model organisms ranging from archaea to eukaryotes using in silico structural analysis tools. The detailed comparative analysis: regarding their structure, function, cofactor, signal peptide, and catalytic domain along with their catalytic residues of α-amylases in 16 model organisms were discussed in this paper. The comparative studies on alpha (α) amylases' secondary and tertiary structures, multiple sequence alignment, transmembrane helices, physiochemical properties, and their phylogenetic analysis in model organisms were briefly studied. This review has documented the recent trends and future perspectives of industrially important novel thermophilic α-amylases. In conclusion, this review sheds light on the current understanding and prospects of α-amylase research, highlighting its importance as a versatile enzyme with numerous applications and emphasizing the need for further exploration and innovation in this field.

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Aspects and Recent Trends in Microbial α-Amylase: a Review

Cited by 63 publications

References 188 publications

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

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

Production of extracellular α-amylase by single-stage steady-state continuous cultures of Candida wangnamkhiaoensis in an airlift bioreactor

Exploration of computational approaches to predict the structural features and recent trends in α‐amylase production for industrial applications

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