Synthesis of partial glycerides rich in α-linolenic acid efficiently from silkworm pupa oil with immobilized lipase MAS1-H108A

Haipeng Yue,Weifei Wang,Shi He,Bo Yang,Xiaoli Qin,Sentai Liao,Yonghua Wang,Ri Ming Luo

doi:10.1590/fst.58221

Abstract

In this paper the ability of immobilized lipase MAS1-H108A to prepare α-linolenic acid-rich partial glycerides was studied. The effects of different reaction conditions on the yield of Diacylglycerol (DAG) and Monoglyceride (MAG) were investigated, including substrate molar ratio, substrate concentration, temperature and lipase dosage. The highest yield (63.92% of MAG and 30.61% of DAG) was obtained when silkworm pupa oil/glycerol ratio of 1:3, lipase dosage was 50 U/g, substrate concentration was 40% (w/v), at 40 °C. Under the optimal conditions, the scale-up (50 times) and single-stage molecular distillation were carried out to separate DAG and MAG, the yield of MAG in the light phase was 99.18%, and the concentration of DAG in the heavy phase was 89.47%, α-linolenic acid in MAG and DAG accounted for 28.96% and 28.23%, respectively. The results can be shown that the immobilized lipase MAS1-H108A has excellent potential for enzymatic glycerolysis to prepare functional partial glycerides.

Highlights

Lipase can catalyze various reactions, such as hydrolysis, esterification, transesterification, acidolysis, alcoholysis and aminolysis, and has good biological properties (Li et al, 2016)
Immobilized lipase MAS1-H108A showed similar resistance to organic solvents as Novozym 435 (Dalla Rosa et al, 2009), the enzyme activity of them will be reduced in the tert-butanol system
In this study, the catalytic performance was better than that of Novozym 435. This might because the immobilized lipase MAS1H108A has stronger non-position selectivity than Novozym 435 (Wang et al, 2017), which will strengthen catalyze acyl transfer

Summary

Introduction

Lipase can catalyze various reactions, such as hydrolysis, esterification, transesterification, acidolysis, alcoholysis and aminolysis, and has good biological properties (Li et al, 2016). Partial glycerides were prepared by enzymatic glycerolysis in solvent-free systems, organic solvent systems, supercritical CO2 systems and the addition of surfactants. Li Yue et al (Li et al, 2018) used Candida antarctica lipase B to catalyze the glycerolysis of soybean oil for 24 h in a solvent-free system, the yields of DAG and MAG were 64.28% and 20.15%, respectively. Valério et al (2010) explored the use of immobilized lipase (Novozym 435) and the surfactant (Tween 65) to produce MAG and DAG from emulsified the two reactants into reverse micelles (glycerol-in-oil) before using Lipozyme 435 enzymatic glycerolization of fish oil to improve the process efficiency of the SC-CO2 medium and the mass transfer of glycerol/oil in the three-phase system, and produced about 75% of MAG and DAG within 1 h. It was not difficult to see that the types and reaction efficiency of lipases available in the process of preparing partial glycerides by enzymatic glycerolysis were two major problems.

Methods

Results

Conclusion