Characterization of new β-galactosidase from acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1

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

doi:10.1016/j.jbiosc.2013.03.012

Cited by 17 publications

(11 citation statements)

References 23 publications

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“…1). comparison with the substrate specificity of the b-D-galactosidase studied in our previous report (7). The enzyme exhibited highest activity for 4-NPFU, and the relative activities for 4-NPGA and 2-NPGA were 87% and 32%, respectively, of that for 4-NPFU.…”

Section: Resultsmentioning

confidence: 58%

“…has a molecular mass of 250 kDa and is composed of two identical subunits. The b-D-galactosidase from T. acidotherma AIU BGA-1, which exhibits optimal activity at pH 3.0e4.0, has a molecular mass of 140 kDa and is composed of two heterosubunits of 86 and 50 kDa (7). The structure of the enzyme purified here also clearly differed from those of A. niger (10), Penicillium multicolor (14), Aspergillus fonsecaeus (12), A. carbonarius (4) and Bispora sp.…”

Section: Originmentioning

confidence: 85%

“…acidotherma AIU BGA-1 was incubated with the lactose medium, pH 4.0, consisting of 2.0% lactose, 0.2% corn steep liquor, 0.2% HH 4 NO 3 , 0.1% KH 2 PO 4 , 0.1% Na 2 HPO 4 , 0.05% MgSO 4 $7H 2 O, 0.15% Ca(NO 3 ) 2 $4H 2 O and 0.1% FeCl 3 $6H 2 O, at 30 C for 4 days according to the procedure described in our previous report (7).…”

Section: Chemicalsmentioning

confidence: 99%

“…The lactose-hydrolyzing activity of b-D-galactosidase was assayed using glucose oxidase according to the method described in our previous report (7).…”

Section: Assay Of Enzyme Activitymentioning

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: 58%

Section: Originmentioning

confidence: 85%

Section: Chemicalsmentioning

confidence: 99%

“…The lactose-hydrolyzing activity of b-D-galactosidase was assayed using glucose oxidase according to the method described in our previous report (7).…”

Section: Assay Of Enzyme Activitymentioning

confidence: 99%

See 2 more Smart Citations

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

Self Cite

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“…However, there are many reports concerning galactosidase production induced with lactose or its derivatives, such as in the fungus Trichoderma sp. which reached 0.35 to 2.24 U/mL (Akinola et al, 2012); Teratosphaeria acidotherma AIU BGA-1 produced four intracellular -D-galactosidases using lactose as a carbon source (Isobe et al, 2013). In this study, T. longibrachiatum produced significant amounts of galactosidase using alternative carbon sources, with enzymatic activities ranging from 1.46 to 17.53 U/mL.…”

Section: Influence Of Agro-industrial Waste On the Production Of Fungmentioning

confidence: 52%

Improved production of -galactosidase and -fructofuranosidase by fungi using alternative carbon sources

Diandra¹,

Vanessa²,

Oriente³

et al. 2015

Sci. Res. Essays

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The influence of alternative carbon sources as inducers of -galactosidase and -fructofuranosidase by filamentous fungi (that are, Aspergillus aculeatus, Chrysonilia sitophila, Gliocladium virens, Aspergillus fumigatus and Trichoderma longibrachiatum), recently isolated from Brazil's Atlantic Forest biome has been investigated. The greatest levels of intracellular β-galactosidase activity were obtained using orange peel waste (56.31 U/mL) with A. aculeatus, rice straw (22.57 U/mL) with G. virens, sorghum straw (16.48 U/mL) with C. sitophila, and passion fruit peel with either A. fumigatus (17.26 U/mL) or T. longibrachiatum (17.53 U/mL). The most effective intracellular -fructofuranosidase activity was obtained by A. aculeatus using trub (409.46 U/mL) or passion fruit peel (44.59 U/mL). Thus, alternative carbon sources, such as orange peel and trub, exhibit great potential as inducers for the production of these enzymes. Such fungal isolates from the Atlantic Forest of Paraná, Brazil are promising candidates for generating significant amounts of β-galactosidase and -fructofuranosidase using abundant and inexpensive agro-industrial substrates.

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Chemistry and Sources of Lactase Enzyme with an Emphasis on Microbial Biotransformation in Milk

Niamah

Al‐Sahlany

Verma

et al. 2023

Microbial Bioreactors for Industrial Molecules

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Characterization of new β-galactosidase from acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1

Cited by 17 publications

References 23 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

Improved production of -galactosidase and -fructofuranosidase by fungi using alternative carbon sources

Chemistry and Sources of Lactase Enzyme with an Emphasis on Microbial Biotransformation in Milk

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