Comparison of the Properties of Lipase Immobilized Onto Mesoporous Resins by Different Methods

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Comparison of the Properties of Lipase Immobilized onto Mesoporous Resins by Different Methods

Wenqin Wang · Yanjun Jiang · Liya Zhou ·Jing Gao*

DepartmentofBioengineering,SchoolofChemicalEngineering,HebeiUniversityofTechnology,Tianjin300130,China

Corresponding author: Jing Gao

E-mail:

Telephone:+86-22-60204293

1. Table

TableS1 The parameters of mesoporous polystyrene resins

resins / particle size (mm) / polarity / functional group / specific surface area
(m2/g) / Average pore diameter
(nm)
NKA-9 / 0.3–1.25 / polar / -CN / 250–290 / 15.5–16.5
S-8 / 0.3–1.25 / strongly polar / -NH2 / 100–120 / 28–30

These data were provided by Tianjin Nankai Hecheng S&T Co.,Ltd.

2. Figuresand Figure Captions

Fig. S1 pH stability of free and immobilized lipase.

The free and immobilized lipase were incubated in PBS (0.1 M adjusted by addition of HCl or NaOH solution) in the pH range of 3.0–9.0 for 10 h at room temperature. Then the hydrolytic activity was determined at the optimum pH 8.0. The highest activity of the lipase after treatment was defined as 100%, and the others were showed as percentages of its activity relative to the highest activity.

Fig. S2 Thermal stability of free and immobilized lipase.

The free and immobilized lipase were incubated in PBS (pH 7.5, 0.1 M) at varying temperatures in the range of 20–60 °C for 2 h. Then the hydrolytic activity was measured at its optimum reaction temperature.The highest activity after incubation was defined as 100%.

Fig. S3 Reusability of immobilized lipase.

The reusability of the immobilized lipase was assessed by catalyzing the hydrolysis of olive oil repeatedly under the following conditions: immobilized lipase (200 mg), PBS (5 mL, pH 8.0, 0.1 M), 40 °C and 150rpm.At each end of the reaction, immobilized lipase was isolated from the oil–water mixture and washed with acetone and then PBS (pH 8.0, 0.1M), following used in the next reaction. The activity in the first run was defined as 100%.

Fig. S4 Storage stability of free and immobilized lipase.

The free and immobilized lipasewere stored at 4 °C for a period of time before determination. Free and immobilized lipase were stored in the formof lipase solution and the dry particles, and the residual activity was determined every 5 days.The initial activity was considered to be 100%.

Fig. S5 N2adsorption/desorptionisotherms of immobilized lipase on resins S-8 (curvea) and NKA-9 (curve b).

Fig. S6 The poresizedistribution of immobilized lipase on resins S-8 (curve a) and NKA-9 (curve b).