Abstract
Backgroundα-Galactosidase is widely distributed in plants, microorganisms, and animals, and it is produced by different fungal sources. Many studies have confirmed the valuable applications of α-galactosidase enzymes for various biotechnological purposes, like the processing of soymilk. ResultsAspergillus niger NRC114 was exploited to produce the extracellular α-galactosidase. One factor per time (OFT) and central composite design (CCD) approaches were applied to determine the optimum parameters and enhance the enzyme production. The CCD model choices of pH 4.73, 1.25% mannose, 0.959% meat extract, and 6-day incubation period have succeeded in obtaining 25.22 U/mL of enzyme compared to the 6.4 U/mL produced using OFT studies. Treatment of soymilk by α-galactosidase caused an increase in total phenols and flavonoids by 27.3% and 19.9%, respectively. Antioxidant measurements revealed a significant increase in the enzyme-treated soymilk. Through HPLC analysis, the appearance of sucrose, fructose, and glucose in the enzyme-treated soymilk was detected due to the degradation of stachyose and raffinose. The main volatile compounds in raw soymilk were acids (45.04%) and aldehydes (34.25%), which showed a remarkable decrease of 7.82% and 20.03% after treatment by α-galactosidase. ConclusionsTo increase α-galactosidase production, the OFT and CCD approaches were used, and CCD was found to be four times more effective than OFT. The produced enzyme proved potent enough to improve the properties of soymilk, avoiding flatulence and undesirable tastes and odors. Graphical Abstract▪
Highlights
Introduction αGalactosidases (EC 3.2.1.22) are enzymes that degrade the terminal α-linked galactoside residues from melibiose, raffinose, and stachyose, which are the main oligosaccharide sugars in many legumes and their products [1]
The enzyme can be exploited in different biomedicine aspects as blood group conversion, treatment of Fabry disease [4], and removal of α-gal-type immunogenic epitopes in xenotransplantation [5, 6]. α-Galactosidase (α-Gal) is not secreted in humans, and the presence of raffinose and stachyose in legumes such as soybeans could hinder digestion and cause flatulence since they are utilized by gas-generating intestinal microorganisms [7]
Isolate identification and localization of α‐galactosidase in A. niger NRC114 Developing Aspergillus niger conidiophores which are characteristic of Aspergillus species were recognized by scanning electron micrograph (SEM) (Fig. 1a, b)
Summary
Introduction αGalactosidases (EC 3.2.1.22) are enzymes that degrade the terminal α-linked galactoside residues from melibiose, raffinose, and stachyose, which are the main oligosaccharide sugars in many legumes and their products [1]. Α-Galactosidase (α-Gal) is not secreted in humans, and the presence of raffinose and stachyose in legumes such as soybeans could hinder digestion and cause flatulence since they are utilized by gas-generating intestinal microorganisms [7] The use of this enzyme to improve the quality of soy products and other legumes is promising through reducing the antinutritional and allergic compounds that exist. Considering microbial enzymes are more stable than plant and animal enzymes, they serve an important role in the food industry They may be manufactured in a cost-effective manner with reduced time and space requirements using fermentation processes, and because of their high consistency, process adjustment and optimization can be done very [9]. Many researchers were interested to produce α-galactosidase from fungal sources such as Aspergillus oryzae [16], Fusarium moniliforme NCIM 1099 [17], and Rhizopus oryzae strain SUK [18]
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