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Table 2 Summary of the conditions for enzyme immobilization and the resulting enzyme reusability

From: Innovative approach for semi‐continuous production of puerarin palmitate via transesterification with novel immobilized lipase

Source

Support

Method

Product

Reaction time; conversion rate

Reusability

Refs.

Lipase from Candida Antarctica

ECR 8806 M (octadecyl functionalized hydrophobic resin)

Adsorption

Phloridzin oleate, naringin oleate, esculin oleate

72 h;

76.93%,

75.43%,

78.11%

 ≥ 70%,

 ≥ 60%,

 ≥ 40%

(15 cycles)

[41]

Lipase from porcine pancreas

Activated carbon (from tamarind seeds)

Covalent binding (glutaraldehyde)

Butyl butyrate

4 h;66.26%

 ≥ 86% (5 cycles)

[45]

Lipase from Thermomyces lanuginosus

Immobead 150

Covalent binding (ethylenediamine)

Butyl butyrate, isoamyl butyrate

24 h; 60%

N/A

[35]

Lipase from Candida antarctica

MSU‐H silica

Covalent binding (glutaraldehyde)

Ethyl ester of conjugated linoleic acid

32 h; 46.9%

 ≥ 90% (4 cycles)

[46]

Lipase from Thermomyces lanuginosus

Silica gel

Covalent binding (glutaraldehyde)

Puerarin palmitate

3 h; 97.17%

 ≥ 95% (4 cycles)

 ≥ 20% (11 cycles)

This study