This paper reports on novel and efficient enhancement effects of fruit juice aroma using immobilized β-glucosidase, the enzyme involved in important functions in living organisms, onto superparamagnetic nanoparticles Fe3O4 via carbodiimide β-glucosidase was purified from mandarin (Citrus reticulata) using ammonium sulfate precipitation and hydrophobic interaction chromatography. To be used in this study, superparamagnetic nanoparticles were synthesized and then the shape, size, and magnetism properties of the nanoparticles were characterized. The purified enzyme was immobilized on the nanoparticles. The optimum temperature for β-glucosidase (40 ℃) was increased by 10 ℃ after immobilization, while the optimum pH values of free and immobilized β-glucosidase were 5.5. While the Km and Vmax values of the free enzyme were 0.264 mM and 294 EU, immobilized enzyme’s Km and Vmax were 0.222 mM and 370 EU, respectively. In addition, it was determined that the storage stability of the immobilized enzyme was higher than the free enzyme. When the effect of some metal ions on the enzyme activity was examined, it was observed that Fe+2 increased the enzyme activity while other metals inhibited it. According to the results obtained, the immobilized enzyme had a flavor-enhancing effect on mandarin juice.

Aims: Determination of the biochemical properties of β-glucosidase in peppermint, which is rich in aromatic compounds. Study Design: β-glucosidase was purified from mint, and biochemical characterization of the purified enzyme was performed. Place and Duration of Study: This study was carried out in the Faculty of Arts and Sciences Biochemistry laboratory. Methodology: Enzyme purification was performed by hydrophobic interaction chromatography using a Sepharose 4B-L-tyrosine-1-naphthylamine gel. Optimum pH, temperature, and substrate specificity of the purified enzyme were determined. The effects of glucose, δ-gluconolactone and some heavy metals on the enzyme activity were investigated. Results: The enzyme was purified with 8-fold and 28% yield. The purified protein from mint was visualized at 65 kDa on SDS-PAGE. The substrate specificity of the purified β-glucosidase from mint was determined against para- and ortho-nitrophenyl β-D-glucopyranoside (p/o-NPG) substrates. The Km values were 0.4 and 0.9 mM, and the Vmax values were 102.2 EU and 96.6 EU, respectively. While the optimum pH for the purified enzyme was 6, the optimum temperature was 35°C. Effects of heavy metals Ag+2, Fe+3, Zn+2, Cu+2, and Pb+2 on the purified enzyme activity were investigated. Relative activities of heavy metals were introduced into the reaction medium as 0.75 mM samples without any known inhibitors in the environment. Fe+3 increased the enzyme activity, and Ag+2, Pb+2, Cu+2, and Zn+2 inhibited the enzyme, and their relative activities were 78, 76, 22, and 31%, respectively. Glucose and δ-gluconolactone competitively inhibited the enzyme activity when p-NPG was the substrate. Ki values of glucose and δ-gluconolactone were determined as 0.034±0.001 and 0.038±0.002 mM, respectively. Conclusion: Determination of the biochemical properties of β-glucosidase from mint, which has commercial and pharmacological importance due to the phenolic substances it contains, will contribute to studies on improving food quality.

Leukocytes are isolated by centrifugation after specific lysis of erythrocytes

β-Glucosidase was purified from Brassica oleracea by salting out with ammonium sulfate and hydrophobic interaction chromatography. Results demonstrated that the enzyme is a dimer (130 kD) made up of one major (80 kD) and one minor subunit (50 kD). The pH optimum is 6.0, with 50% of the enzyme's original activity remaining between pH 4.0 and pH 7.0. The temperature optimum is 35C, and activity did not decrease after two hours of exposure to this temperature. The activity of the enzyme was investigated on four substrates, 4-Nitrophenyl β-D-glucopyranoside (p-NPG), ortho-Nitrophenyl-β-D-glucopyranoside (o-NPG), para-Nitrophenyl-β-D-galactoside (p-NPGal) and ortho-Nitrophenyl-β-D-galactoside (o-NPGal), and km values were shown to be 0.755 mM, 0.174 mM, 0.988 mM and 0.213 mM, while Vmax values were 604 U/mg, 38 U/mg, 556 U/mg and 308 U/mg, respectively. The enzyme is completely inhibited by gluconolactone and glucose against p-NPG as substrate, with ki values of 0.038 mM and 0.64 mM, respectively. To our knowledge, this is the first study demonstrating purification and characterization of β-glucosidase from broccoli, thus providing a better understanding of its role in the plant, and establishing a basis for further research. Practical Applications To our knowledge, this is the first study demonstrating purification and characterization of β-glucosidase from broccoli, thus providing a better understanding of its role in the plant, and establishing a basis for further research. The results of this research highlight the potential of the enzyme isolated from broccoli for further research. Succeeding efforts would involve optimization of this procedure for increasing the enzyme yield, in order to make it a viable candidate for industrial application.

Gaucher disease is a hereditary genetic abnormality which defects the pathway of sphingolipid catabolism. The mutation of GBA gene which encodes lysosomal β-glucosidase enzyme is the main characteristics of the disease also is observed in different cancer types. To find the relation between the disease and colon adenocarcinoma, the responsible gene expression of Gaucher disease was analyzed. The gene expression of colon adenocarcinoma was was compared between death and alive patients and analyzed statistically to profile the differences between Gaucher disease genes expression changes. GBA, GBA2, GBA3, SCARB2 and PSAP have the maximum genetic alteration which is observed in colon adenocarcinoma.