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Volume 92, Issue 2 , Pages 491-498 , February 2009

Immobilization of recombinant thermostable β-galactosidase from Bacillus stearothermophilus for lactose hydrolysis in milk

W. Chen
- State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
- Corresponding author.
H. Chen
- State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
Y. Xia
- State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
J. Yang
- State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
J. Zhao
- State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
F. Tian
- State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
H.P. Zhang
- Key Laboratory of Dairy Biotechnology and Engineering, Ministry of Education, Inner Mongolia Agricultural University, Huhhot, Inner Mongolia 010018, P. R. China
H. Zhang
- State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China

Received 11 August 2008 ,Accepted 22 October 2008.

Effects of temperature on relative enzyme activity of free and immobilized enzymes. ■ = Tris(hydroxymethyl)phosphine (THP)-immobilized enzyme; ▴ = glutaraldehyde-immobilized enzyme; ● = free enzyme.

Effects of temperature on relative enzyme activity of free and immobilized enzymes. ■ = Tris(hydroxymethyl)phosphine (THP)-immobilized enzyme; ▴ = glutaraldehyde-immobilized enzyme; ● = free enzyme.
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Effects of pH on relative enzyme activity of free and immobilized enzymes. ■ = Tris(hydroxymethyl)phosphine (THP)-immobilized enzyme; ▴ = glutaraldehyde-immobilized enzyme; ● = free enzyme.

Effects of pH on relative enzyme activity of free and immobilized enzymes. ■ = Tris(hydroxymethyl)phosphine (THP)-immobilized enzyme; ▴ = glutaraldehyde-immobilized enzyme; ● = free enzyme.
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Effects of reuse times on residual activity of immobilized enzymes. The white and black bars represent the glutaraldehyde- and tris(hydroxymethyl)phosphine (THP)-immobilized enzymes, respectively.

Effects of reuse times on residual activity of immobilized enzymes. The white and black bars represent the glutaraldehyde- and tris(hydroxymethyl)phosphine (THP)-immobilized enzymes, respectively.
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Storage and thermostability of free and immobilized enzymes: Storage at A) 4°C; B) 60°C; C) 65°C; and D) 70°C (A to D from top to bottom). ■ = Tris(hydroxymethyl)phosphine (THP)-immobilized enzyme; ▴

Storage and thermostability of free and immobilized enzymes: Storage at A) 4°C; B) 60°C; C) 65°C; and D) 70°C (A to D from top to bottom). ■ = Tris(hydroxymethyl)phosphine (THP)-immobilized enzyme; ▴ = glutaraldehyde-immobilized enzyme; ● = free enzyme.
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Hydrolysis of lactose in milk by Tris(hydroxymethyl) phosphine (THP)-immobilized β-galactosidase in a packed bed reactor at 70°C (■) at a flow rate of 0.8 mL/min, (▴) at a flow rate of 1.3 mL/min.

Hydrolysis of lactose in milk by Tris(hydroxymethyl) phosphine (THP)-immobilized β-galactosidase in a packed bed reactor at 70°C (■) at a flow rate of 0.8 mL/min, (▴) at a flow rate of 1.3 mL/min.
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