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In this study, an amyloglucosidase from L. More recently, this enzyme has been reported to be produced from some microorganisms, viz, Aspergillus flavus (Karim et al. shimeji, stating that the enzyme was most active at around 40 ☌. 2004 characterized an extracellular glucoamylase from L. 2011), as well as in two ectomycorrhizal fungi, Tricholoma matsutake and Lyophyllum shimeji (Hur et al. Glucoamylase has been reported in Rhizopus oryzae (Morita and Fujio, 2000), Aspergillus awamori (Negi and Banerjee 2009), Aspergillus niger (Slivinski et al. Consequently, AMG can be considered as an economically significant enzyme because of its effectiveness in hydrolyzing starch and some oligosaccharides into β- d-glucose. AMG serves as a raw material for fermentation in the production of ethanol, glucose syrups, and in some cases can be used to improve barley mash for beer production (Aiyer 2005 Zambare 2010). Amylose is a linear chain of glucose residues linked by α-1,4 bonds while amylopectin is a branched polymer with α-1,4-linked and α-1,6-linked glucose residues. It is made up of two molecular weight polymers, amylose and amylopectin. Starch is one of the most abundantly distributed polysaccharides produced by plants. It is also an exo-acting enzyme that catalyzes the production of β- d-glucose from the non-reducing ends of substrates that include starch, and maltooligosaccharides by consecutively hydrolyzing α-1,4 and α-1,6 linkages (Sauer et al. Amyloglucosidase (AMG, glucoamylase, EC 3.2.1.3) is an enzyme that is capable of hydrolyzing the α-1,4 glycosidic bonds from the non-reducing ends of starch to produce glucose. Alpha-amylases are exo-acting enzymes that randomly cleave the 1,4-α- d-glucosidic linkages between adjacent glucose units in the linear amylose chain. 2018).Īlpha-amylase and glucoamylase are the two major classes of amylases, mostly identified among microorganisms (John 2017). The application of amylases has increased over the years in areas such as juice processing, processing of starch, resizing of textiles, paper sizing, detergent additives, malting barley and bakery industries (Singh et al. Some of the desired characteristics of industrial enzymes include thermostability, specificity and pH stability. A new area of biotechnological research now focuses on the production and characterization of enzymes from various sources with unique properties (Karim et al. Other reports have also indicated that the enzymatic degradation of organic polymers in the soil and the transfer of some of the resulting products to the root is a significant benefit to the growth and development of ericaceous plants (Smith and Read 2008). Ericoid mycorrhizal (ERM) fungi have been found to produce hydrolytic enzymes (Cairney and Burke 1994, 1998) which include the production of amyloglucosidase. The survival of ericaceous plants in nutrient–deficient soils depends strongly on the symbiotic association that exists between them and mycorrhizal fungi, where nutrients are made available from soil organic matter through the assistance of hydrolytic enzymes. Ericaceous plants belong to a family of plants that can alter their physiological or morphological characteristics in nutrient deficient ecosystems. Leohumocola incrustata is a genus of mycorrhizas commonly found within the roots of ericaceous plants. Also, this study reports for the first time the possibility of using some culturable ERM fungi to produce enzymes for the bio-economy. incrustata is a glucoamylase with promising characteristics such as temperature stability over an extended period, high substrate affinity and stability to a range of chemicals. Thin layer chromatography revealed that only glucose was produced as the product of starch hydrolysis. The metal inhibition profile of the AMG showed that Mn 2+ and Ca 2+ enhanced activity, while it was stable to metals ions, except a few (Al 3+, Co 2+, Hg 2+ and Cd 2+) that were inhibitory at a concentration higher than 5 mM. The enzyme was stable at 45 ☌ (pH 5.0), retaining over 65% activity after a pre-incubation period of 24 h. The K m and k cat values were 0.38 mg mL −1 and 70 s −1, respectively, using soluble starch as a substrate. The molecular mass of the AMG was estimated to be 101 kDa by combining the results of Sephadex G-100 gel filtration, sodium dodecyl sulphate–polyacrylamide gel electrophoresis, and zymography. AMG was purified to homogeneity from cell-free culture filtrate of an ERM fungus grown in a modified Melin–Norkrans liquid medium. This study aimed to purify and characterize amyloglucosidase (AMG) from Leohumicola incrustata.