In this work, a lipase–glucose oxidase system has been designed and proven to be an efficient system for the oxidation of N-heteroaromatic compounds and tertiary amines. This dual-enzyme system not only displays environmental friendliness, but also demonstrates its huge potential in industrial applications.

The present work illustrates the condensation of substituted salicylaldehyde and malononitrile catalyzed by lipase under microwave irradiation. The reaction obtains two different products by a delicate control of the substrate molar ratio and reaction time. This protocol has the advantages of high yield, short reaction time and environmental friendliness.

The synthesis of benzo[g]chromene derivatives through a multi-component reaction catalyzed by lipase is reported for the first time. This novel efficient method has the advantages of environmental friendliness, high yield and simple work-up. Moreover, this protocol extends the phenomenon of enzyme promiscuity.

A new method for the enamination of 1,3-dicarbonyl compounds catalyzed by laccase in water is described for the first time. Besides providing a green and efficient method for the synthesis of enaminones, this study extends the applicability of laccase in organic synthesis.

A new method for the synthesis of substituted 2H-chromenes catalyzed by lipase was reported in the first time. Besides providing a simple and efficient method for the synthesis of 2H-chromenes, this study extends the applicability of lipase in organic synthesis.

As a green and inexpensive biocatalyst, lipase has been used to catalyze the synthesis of 3,3′-(arylmethylene)bis(2-hydroxynaphthalene-1,4-dione) (3) for the first time. The products could be obtained in excellent yields (82.2–94.8%, 2 h). This study not only provides a simple and efficient method, but also expands the biocatalytic promiscuity of lipase in organic synthesis.

A simple and efficient Knoevenagel condensation between α,β-unsaturated aldehydes and active methylene compounds is reported. Notably, this condensation can be catalyzed by PPL (lipase from porcine pancreas) with satisfied yields (49%–92%). Moreover, PPL induces moderate Z/E selectivity in the Knoevenagel condensation.A simple and efficient Knoevenagel condensation between α,β-unsaturated aldehydes and active methylene compounds is reported. This reaction can be catalyzed by PPL (lipase from porcine pancreas) with satisfied yields (49%–92%) and moderate Z/E selectivity.

The lipase from Pseudomonas fluorescens (Lipase AK, AKL) was immobilized onto the magnetic Fe3O4 nanoparticles via hydrophobic interaction. Enzyme loading and immobilization yield were determined as 21.4 ± 0.5 mg/g and 49.2 ± 1.8 %, respectively. The immobilized AKL was successfully used for resolution of 2-octanol with vinyl acetate used as acyl donor. Effects of organic solvent, water activity, substrate ratio, and temperature were investigated. Under the optimum conditions, the preferred isomer for AKL is the (R)-2-octanol and the highest enantioselectivity (E = 71.5 ± 2.2) was obtained with a higher enzyme activity (0.197 ± 0.01 μmol/mg/min). The results also showed that the immobilized lipase could be easily separated from reaction media by the magnetic steel and remained 89 % of its initial activity as well as the nearly unchanged enantioselectivity after five consecutive cycles, indicating a high stability in practical operation.

Aeropyrum pernix esterase (APE1547) was successfully used to catalyze the enantioselective transesterification of (R/S)-2-methyl-1-butanol in an ionic liquid (IL). Effects of various reaction conditions on the synthetic activity of the enzyme as well as enantioselectivity, including the type of IL, acyl donor, temperature, water activity, and substrate molar ratio were inverstigated. APE1547 showed good catalytic performance (activity > 0.8 μmol/min/mg, E > 25), and the enzyme-IL mixture was recycled five times with only a slight decrease in catalytic performance.

Recently, significant efforts have been devoted into the study of the effect of hydrophobic supports on the catalytic properties of immobilized lipases. It seems that immobilization lipases on hydrophobic supports is a simple and efficient method to improve the catalytic activity of lipases. In this study, the hydrophobic poly(N-propyl-norbornene-exo-2,3-dicarboximide)s with well-controlled molecular weight were synthesized by the living ring-opening metathesis polymerization, and the lipases from Pseudomonas sp. were then immobilized on these hydrophobic polymer supports through the physical adsorption. The immobilized lipases exhibited higher activity and enantioselectivity for the transesterification of 2-octanol than those of free lipases. Furthermore, we investigated the polymer molecular weight-mediated catalytic properties of immobilized lipases. It was found that the catalytic activity and E value of the immobilized lipases increased with the increase of the polymer molecular weight. At the polymeric molecular weight of about 40kDa, the highest E value (58 at 54.2% of conversion, enantiomeric excess = 99%) was reached. After the molecular weight of polymers getting higher than 40 kDa, catalytic activity and E value of the immobilized lipase decreased.