Acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1, produces multiple forms of intracellular β-galactosidase

Isobe, Kimiyasu; Takahashi, Naomi; Chiba, Serina; Yamashita, Manabu; Koyama, Takahumi

doi:10.1016/j.jbiosc.2013.02.018

Cited by 15 publications

(12 citation statements)

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“…Purification and molecular mass We demonstrated in our previous report that the b-D-galactosidases from T. acidotherma AIU BGA-1 were separated into three peaks by DEAE-Toyopearl column chromatography, and the active fractions containing acidophilic enzymes were further separated into two peaks by PhenylToyopearl column chromatography (6). On the basis of these previous results, we purified the second acidophilic enzyme to an electrophoretically homogeneous state according to the procedure described above in Materials and methods using six column chromatographies (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…These enzymes are also utilized as digestive supplements for lactose-intolerant individuals (4,5). Recently, we isolated Teratosphaeria acidotherma AIU BGA-1 as a new producer of b-D-galactosidase, and revealed that this strain produced three acidophilic b-D-galactosidases and one alkalophilic b-D-galactosidase with different pH activity profiles (6). Then, we purified one of the acidophilic b-D-galactosidases [P-4 in our previous report (6)] from the strain, and revealed that the enzyme exhibited high activity and stability in a wide pH range from the acidic region to the neutral region, but did not exhibit high activity and stability at pH 1.0 (7).…”

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confidence: 99%

“…Recently, we isolated Teratosphaeria acidotherma AIU BGA-1 as a new producer of b-D-galactosidase, and revealed that this strain produced three acidophilic b-D-galactosidases and one alkalophilic b-D-galactosidase with different pH activity profiles (6). Then, we purified one of the acidophilic b-D-galactosidases [P-4 in our previous report (6)] from the strain, and revealed that the enzyme exhibited high activity and stability in a wide pH range from the acidic region to the neutral region, but did not exhibit high activity and stability at pH 1.0 (7). Here, we purified the other acidophilic b-Dgalactosidase with high activity in the extremely acidic pH region [F-2 in our previous report (6)] from the same strain to compare some of its characteristics with the other microbial b-D-galactosidases.…”

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confidence: 99%

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Novel acidophilic β-galactosidase with high activity at extremely acidic pH region from Teratosphaeria acidotherma AIU BGA-1

Chiba

Yamada

Isobe

2015

Journal of Bioscience and Bioengineering

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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Novel acidophilic β-galactosidase with high activity at extremely acidic pH region from Teratosphaeria acidotherma AIU BGA-1

Chiba

Yamada

Isobe

2015

Journal of Bioscience and Bioengineering

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“…However, the enzyme activity was found to be significantly activated in the presence of 15–30% NaCl concentration. In another study, β‐galactosidase exhibiting high activity in an extremely acidic pH region to neutral pH region was efficiently purified by Isobe, Naomi, Serina, Miho, and Takahumi () from an acidophilic fungus, Teratosphaeria acidotherma AIU BGA‐1isolated from an acidic and high temperature hot spring. Four intracellular β‐ d ‐galactosidases were produced with different pH activity profiles, in which three were acidophilic and one was alkalophilic in nature.…”

Section: Fungal and Yeast Enzyme Sources Of β‐Galactosidasementioning

confidence: 99%

β-galactosidase: Biotechnological applications in food processing

2018

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β‐Galactosidases produced by microorganisms are being used in food technology for hydrolysis of lactose in milk and milk by‐products. The enzyme has attracted much attention in view of lactose intolerance in human population and due to importance of milk in human diet. β‐Galactosidase hydrolyze β‐galactopyranosides, that is, lactose, and form a range of trans‐galactosylation products or galactooligosaccharides (GOS) capable of providing several health benefits as prebiotics. In addition, the enzyme also finds applications in production of lactose based sweeteners from high lactose containing effluents of cheese manufacturing industries. Currently, the enzyme is mainly obtained from Aspergillus niger and Kluyveromyces lactis, however, they are thermolabile with optimum pH between 4.0 and 6.0 accompanied by low chemical resistance and high product inhibition properties. Thermostable enzymes are suitable to perform the hydrolytic process at relatively high temperatures, minimizing pathogen contamination, psychrophilic β‐galactosidases are preferred for treatment of milk under refrigerated conditions (<15°C), without heating and maintenance of temperature. Lactic acid bacteria (LAB) are a potential source of food grade enzymes and other metabolites. Although reports on the use of β‐galactosidase of LAB in pure form is reported for hydrolysis of lactose in milk and production of fermented milk products for reduced lactose content, methods of immobilization for use in continuous bioreactors are less explored. Recombinant DNA technology has attained much significance to reveal molecular aspects of enzyme catalysis, protein structure, gene organization for expression, and enhancement of thermophilic, psychrophilic, and mesophilic β‐galactosidases. Heterologous expression of extremozymes with β‐galactosidase would help in overcoming the limitations faced within the bioprocess technology. Practical applications Lactic acid bacteria (LAB) producing extracellular cell bound β‐galactosidase have been isolated and enzyme production was carried out using modified MRS medium incorporating lactose as enzyme inducer. Process for growing probiotic lactic acid bacteria for β‐galactosidase from fermented milk products has been patented (Indian Patent No. 247904). Thermostable β‐galactosidases were also extracted from Kluyveromyces lactis a yeast, isolated from curd samples and Bacillus sp. MTCC 864. An Indian patent has been granted for a simple, cost effective perforated two compartment immobilized enzyme bioreactor was designed and fabricated for lactose hydrolysis (Indian Patent No. 264609). The bioreactor can be operated continuously at temperature between 5.0 and 75.0°C, employing different immobilized enzyme preparations for different operational temperatures. β‐galactosidase of cell confined LAB and yeast have been immobilized in agarose and galactooligosaccharides (GOS) production was observed at 40% lactose concentration in 0.05M phosphate buffer at pH 6.5. Immobilized bioreactor preparation could be used for lactos...

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“…A large number of microorganisms have been assessed as potential sources of β- d -galactosidase (β- d -galactoside galactohydrolase, EC 3.2.1.23, most commonly known as lactase) to hydrolyze lactose into glucose and galactose for lactose-free milk production and products intended for lactose-intolerant consumers (Isobe et al 2013a). Traditionally, the β-galactosidases most widely used in industry were obtained from Aspergillus spp.…”

Section: Introductionmentioning

confidence: 99%

Optimization and partial purification of beta-galactosidase production by Aspergillus niger isolated from Brazilian soils using soybean residue

et al. 2019

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β-Galactosidases are widely used for industrial applications. These enzymes could be used in reactions of lactose hydrolysis and transgalactosylation. The objective of this study was the production, purification, and characterization of an extracellular β-galactosidase from a filamentous fungus, Aspergillus niger. The enzyme production was optimized by a factorial design. Maximal β-galactosidase activity (24.64 U/mL) was found in the system containing 2% of a soybean residue (w/v) at initial pH 7.0, 28 °C, 120 rpm in 7 days. ANOVA of the optimization study indicated that the response data on temperature and pH were significant (p < 0.05). The regression equation indicated that the R 2 is 0.973. Ultrafiltration at a 100 and 30 kDa cutoff followed by gel filtration and anion exchange chromatography were carried out to purify the fungal β-galactosidase. SDS-PAGE revealed a protein with molecular weight of approximately 76 kDa. The partially purified enzyme showed an optimum temperature of 50 °C and optimum pH of 5.0, being stable under these conditions for 15 h. The enzyme was exposed to conditions approaching gastric pH and in pepsin’s presence, 80% of activity was preserved after 2 h. These results reveal a A. niger β-galactosidase obtained from residue with favorable characteristics for food industries.

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Acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1, produces multiple forms of intracellular β-galactosidase

Cited by 15 publications

References 15 publications

Novel acidophilic β-galactosidase with high activity at extremely acidic pH region from Teratosphaeria acidotherma AIU BGA-1

Novel acidophilic β-galactosidase with high activity at extremely acidic pH region from Teratosphaeria acidotherma AIU BGA-1

β-galactosidase: Biotechnological applications in food processing

Optimization and partial purification of beta-galactosidase production by Aspergillus niger isolated from Brazilian soils using soybean residue

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