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Production of Galactooligosaccharides Using β-Galactosidase Immobilized on Chitosan-Coated Magnetic Nanoparticles with Tris(hydroxymethyl)phosphine as an Optional Coupling Agent.

Chen SC, Duan KJ - Int J Mol Sci (2015)

Bottom Line: However, activity retention of batchwise reactions was similar for both immobilized systems.All the three enzyme systems produced GOS compound with similar concentration profiles, with a maximum GOS yield of 50.5% from 36% (w · v(-1)) lactose on a dry weight basis.The chitosan-coated magnetic Fe3O4 nanoparticles can be regenerated using a desorption/re-adsorption process described in this study.

View Article: PubMed Central - PubMed

Affiliation: Department of Bioengineering, Tatung University, Taipei 104, Taiwan. monica94707@yahoo.com.tw.

ABSTRACT
β-Galactosidase was immobilized on chitosan-coated magnetic Fe3O4 nanoparticles and was used to produce galactooligosaccharides (GOS) from lactose. Immobilized enzyme was prepared with or without the coupling agent, tris(hydroxymethyl)phosphine (THP). The two immobilized systems and the free enzyme achieved their maximum activity at pH 6.0 with an optimal temperature of 50 °C. The immobilized enzymes showed higher activities at a wider range of temperatures and pH. Furthermore, the immobilized enzyme coupled with THP showed higher thermal stability than that without THP. However, activity retention of batchwise reactions was similar for both immobilized systems. All the three enzyme systems produced GOS compound with similar concentration profiles, with a maximum GOS yield of 50.5% from 36% (w · v(-1)) lactose on a dry weight basis. The chitosan-coated magnetic Fe3O4 nanoparticles can be regenerated using a desorption/re-adsorption process described in this study.

No MeSH data available.


Time-course analysis of various sugars produced. (A) free enzyme; (B) Fe3O4-CS-immobilized; and (C) Fe3O4-CS-THP-immobilized enzyme. The reaction was carried out at 45 °C at pH 6.0 with a 36% lactose solution (w·v−1). 3.5 units of enzyme were added per gram of lactose. (▼) lactose; (●) glucose; (○) galactose; (▽) disaccharide; (■) trisaccharide; (□) tetrasaccharide.
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ijms-16-12499-f007: Time-course analysis of various sugars produced. (A) free enzyme; (B) Fe3O4-CS-immobilized; and (C) Fe3O4-CS-THP-immobilized enzyme. The reaction was carried out at 45 °C at pH 6.0 with a 36% lactose solution (w·v−1). 3.5 units of enzyme were added per gram of lactose. (▼) lactose; (●) glucose; (○) galactose; (▽) disaccharide; (■) trisaccharide; (□) tetrasaccharide.

Mentions: The concentration profiles of glucose, galactose, disaccharides, trisaccharides, and tetrasaccharides were determined in time-course experiments for the free and immobilized enzymes. The results showed that the three systems have similar product profiles (Figure 7). Trisaccharide is the first transgalactosyl product derived from lactose. Tetrasaccharide is the product of transgalactosylating reaction of a galactoside on the trisaccharide. Two disaccharides were produced by transgalactosylating of galactoside on glucose, probably β-d-Gal-(1→3)-d-Glc and β-d-Gal-(1→6)-d-Glc [1].


Production of Galactooligosaccharides Using β-Galactosidase Immobilized on Chitosan-Coated Magnetic Nanoparticles with Tris(hydroxymethyl)phosphine as an Optional Coupling Agent.

Chen SC, Duan KJ - Int J Mol Sci (2015)

Time-course analysis of various sugars produced. (A) free enzyme; (B) Fe3O4-CS-immobilized; and (C) Fe3O4-CS-THP-immobilized enzyme. The reaction was carried out at 45 °C at pH 6.0 with a 36% lactose solution (w·v−1). 3.5 units of enzyme were added per gram of lactose. (▼) lactose; (●) glucose; (○) galactose; (▽) disaccharide; (■) trisaccharide; (□) tetrasaccharide.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4490457&req=5

ijms-16-12499-f007: Time-course analysis of various sugars produced. (A) free enzyme; (B) Fe3O4-CS-immobilized; and (C) Fe3O4-CS-THP-immobilized enzyme. The reaction was carried out at 45 °C at pH 6.0 with a 36% lactose solution (w·v−1). 3.5 units of enzyme were added per gram of lactose. (▼) lactose; (●) glucose; (○) galactose; (▽) disaccharide; (■) trisaccharide; (□) tetrasaccharide.
Mentions: The concentration profiles of glucose, galactose, disaccharides, trisaccharides, and tetrasaccharides were determined in time-course experiments for the free and immobilized enzymes. The results showed that the three systems have similar product profiles (Figure 7). Trisaccharide is the first transgalactosyl product derived from lactose. Tetrasaccharide is the product of transgalactosylating reaction of a galactoside on the trisaccharide. Two disaccharides were produced by transgalactosylating of galactoside on glucose, probably β-d-Gal-(1→3)-d-Glc and β-d-Gal-(1→6)-d-Glc [1].

Bottom Line: However, activity retention of batchwise reactions was similar for both immobilized systems.All the three enzyme systems produced GOS compound with similar concentration profiles, with a maximum GOS yield of 50.5% from 36% (w · v(-1)) lactose on a dry weight basis.The chitosan-coated magnetic Fe3O4 nanoparticles can be regenerated using a desorption/re-adsorption process described in this study.

View Article: PubMed Central - PubMed

Affiliation: Department of Bioengineering, Tatung University, Taipei 104, Taiwan. monica94707@yahoo.com.tw.

ABSTRACT
β-Galactosidase was immobilized on chitosan-coated magnetic Fe3O4 nanoparticles and was used to produce galactooligosaccharides (GOS) from lactose. Immobilized enzyme was prepared with or without the coupling agent, tris(hydroxymethyl)phosphine (THP). The two immobilized systems and the free enzyme achieved their maximum activity at pH 6.0 with an optimal temperature of 50 °C. The immobilized enzymes showed higher activities at a wider range of temperatures and pH. Furthermore, the immobilized enzyme coupled with THP showed higher thermal stability than that without THP. However, activity retention of batchwise reactions was similar for both immobilized systems. All the three enzyme systems produced GOS compound with similar concentration profiles, with a maximum GOS yield of 50.5% from 36% (w · v(-1)) lactose on a dry weight basis. The chitosan-coated magnetic Fe3O4 nanoparticles can be regenerated using a desorption/re-adsorption process described in this study.

No MeSH data available.