“…Moreover, the activity had a maximum at pH 6.0 and this value is higher than the optimum pHs of most mushroom and fungal a-galactosidases (pH 2.5-5.5). [21][22][23][24][25][26] The distinctive characteristic of the G. lucidum a-galactosidase was its extreme thermostability. The optimum temperature of this a-galactosidase is 709 C and the enzyme was fully stable after heating at 709 C for 30 min.…”
“…Moreover, the activity had a maximum at pH 6.0 and this value is higher than the optimum pHs of most mushroom and fungal a-galactosidases (pH 2.5-5.5). [21][22][23][24][25][26] The distinctive characteristic of the G. lucidum a-galactosidase was its extreme thermostability. The optimum temperature of this a-galactosidase is 709 C and the enzyme was fully stable after heating at 709 C for 30 min.…”
“…these enzymes are used in the hydrolysis of raffinose and stachyose present in soy beans and other leguminous food and feed that cause intestinal discomfort, flatulence and low feed utilization in monogastrites (12). In beet sugar industry, α-galactosidases are used to remove raffinose from beet molasses increasing the sucrose yield (23). α-Galactosidase is also used to improve the gelling properties of galactomannans to be used as food thickeners (5).…”
Section: Introductionmentioning
confidence: 99%
“…Abundant information is available on the biosynthesis of α-galactosidase from filamentous fungi belonging to the genera Penicillium and Aspergillus (1,4,6,8,9,16,18,21,23,25,26) during submerged fermentation.…”
“…[7][8][9] We have purified -galactosidases from several species and have determined the substrate specificities of each of them. [10][11][12][13] Umbelopsis vinacea (filamentous fungi, earlier we used the synonym Mortierella vinacea) possesses two types of -galactosidases, and one of which, -galactosidase I (UvGalI), has a molecular mass of 50-56 kDa and 240 kDa when analyzed by SDS-PAGE and gel filtration respectively. The broadness of the SDS-PAGE band suggests that UvGalI might be a heterogeneous glycoprotein.…”
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