Microbial production and biotechnological applications of α-galactosidase

Bhatia, Sonu; Singh, Atinderpal; Batra, Navneet; Singh, Jagtar

doi:10.1016/j.ijbiomac.2019.10.140

Cited by 76 publications

(49 citation statements)

References 203 publications

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“…The biotechnological applications of α-galactosidase includes the removal of raffinose family oligosaccharides (RFOs) in soymilk, beet sugar industry, flatulence, blood group conversion, etc. (Raja et al 2020;Bhatia et al 2019). Carbon occupies a unique position among the essential elements required by microorganisms.…”

Section: Discussionmentioning

confidence: 99%

High-yield production and biochemical characterization of α-galactosidase produced from locally isolated Penicillium sp.

Kote¹,

Manjula²,

Vishwanatha³

et al. 2020

Bull Natl Res Cent

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Background α-Galactosidase is widely used in various biotechnological applications such as food processing, beet sugar, the pulp and paper industries, synthesis of oligosaccharides by trans-galactosylation, hydraulic fracturing of oil and gas wells, and medical applications. Results Screening and identification of fungi for α-galactosidase activity was performed. The isolate Penicillium sp. showed good α-galactosidase activity. α-Galactosidase production by the fungal strain Penicillium sp. cultivated in solid state fermentation (SSF) conditions using copra mannan extract as nutrient medium was investigated. The maximum α-galactosidase activity of 5.391 U/mL was obtained in defatted copra meal (dFCO) as carbon source, which is 2–3% greater as compared with commercial mannans and unprocessed copra meal. The highest product yield of α-galactosidase was obtained with media containing yeast extract (6.672 U/ml) as organic nitrogen and ammonium nitrate (6.325 U/ml) and as inorganic nitrogen source with media pH 5.5, and the time course of enzyme production was at the 5th day of fermentation, respectively. The optimum pH of α-galactosidase was obtained at pH 5 and optimum temperature at 60 °C. The enzyme was stable between pH 4 and 6 and retained more than 50% of residual activity for an 8-h incubation period. The Ca+2 ions enhanced the enzyme activity and Mn+2 ions have not altered the enzyme activity, whereas Hg+2 strongly inhibited the enzyme activity. Conclusions The findings of present investigations on α-galactosidase are of particular interest for its application in the food processing industry.

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Section: Discussionmentioning

confidence: 99%

High-yield production and biochemical characterization of α-galactosidase produced from locally isolated Penicillium sp.

Kote¹,

Manjula²,

Vishwanatha³

et al. 2020

Bull Natl Res Cent

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“…Enzyme activity, carbon source utilization, inhibition, and drug resistance of WangLB bacterium were measured by VITEK 2 BCL card. The results showed that it belonged to Bacillus as it had positive reactions in L-aspartate arylaminase, Leucine arylaminase, phenylalanine arylaminase, L-proline arylaminase, alanine arylaminase, tyrosine arylaminase, alanine phenylalanine proline arylaminase, α-galactosidase [13], β-glucosidase, pyruvate, esculin hydrolysis, tetrazolium red, and resistance to polymyxin B (Table 1).…”

Section: Morphological and Biochemical Identification Of Wanglbmentioning

confidence: 99%

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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“…Considering the specificity of enzymes in targeting polymer links and their stabilities with respect to different environmental conditions, previous studies have investigated several high-performance hydrolase breakers that can specifically degrade the glycosidic bonds of guar-based polymers, such as mannanase, cellulase, galactosidase, and amylase [ 24 , 25 , 26 , 27 , 28 ]. However, the existing literature does not include reports on enzyme breakers with higher gel-breaking efficiency in medium-temperature and alkaline reservoirs.…”

Section: Introductionmentioning

confidence: 99%

Performance Evaluation of Enzyme Breaker for Fracturing Applications under Simulated Reservoir Conditions

et al. 2021

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Fracturing fluids are being increasingly used for viscosity development and proppant transport during hydraulic fracturing operations. Furthermore, the breaker is an important additive in fracturing fluid to extensively degrade the polymer mass after fracturing operations, thereby maximizing fracture conductivity and minimizing residual damaging materials. In this study, the efficacy of different enzyme breakers was examined in alkaline and medium-temperature reservoirs. The parameters considered were the effect of the breaker on shear resistance performance and sand-suspending performance of the fracturing fluid, its damage to the reservoir after gel breaking, and its gel-breaking efficiency. The experimental results verified that mannanase II is an enzyme breaker with excellent gel-breaking performance at medium temperatures and alkaline conditions. In addition, mannanase II did not adversely affect the shear resistance performance and sand-suspending performance of the fracturing fluid during hydraulic fracturing. For the same gel-breaking result, the concentration of mannanase II used was only one fifth of other enzyme breakers (e.g., mannanase I, galactosidase, and amylase). Moreover, the amount of residue and the particle size of the residues generated were also significantly lower than those of the ammonium persulfate breaker. Finally, we also examined the viscosity-reducing capability of mannanase II under a wide range of temperatures (104–158 °F) and pH values (7–8.5) to recommend its best-use concentrations under different fracturing conditions. The mannanase has potential for applications in low-permeability oilfield development and to maximize long-term productivity from unconventional oilwells.

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Microbial production and biotechnological applications of α-galactosidase

Cited by 76 publications

References 203 publications

High-yield production and biochemical characterization of α-galactosidase produced from locally isolated Penicillium sp.

High-yield production and biochemical characterization of α-galactosidase produced from locally isolated Penicillium sp.

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

Performance Evaluation of Enzyme Breaker for Fracturing Applications under Simulated Reservoir Conditions

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