Wheat germ lipase: isolation, purification and applications

Abstract

In recent years, wheat germ lipase (WGL) is attracting considerable interest. To date, several WGL applications have already been described: (i) fats and oils modification; (ii) esterification reactions in organic media, accepting a wide range of acids and alcohols as substrates; (iii) the asymmetric resolution of various chiral racemic intermediates; (iv) more recently, the promiscuous activity of WGL has been shown in carbon-carbon bond formation. To date, no crystallographic structure of this enzyme has been published, which means its activity, catalytic potential and substrate scope is being assessed empirically. Therefore, new catalytic activities of this enzyme are constantly being discovered. Taking into account the emergency and the current interest in environmentally sustainable processes, this review aims to highlight the origin, isolation, stabilization by immobilization and applications of the wheat germ lipase.

HIGHLIGHTS

• Wheat germ as an inexpensive source of biocatalysts

• Wheat germ lipase an efficient catalyst for various chemical transformations

• Wheat germ lipase in food production

• Industrial applications of wheat germ lipase

• Wheat germ lipase as a promiscuous biocatalyst

• Immobilization of wheat germ lipase as a method of stabilization

Keywords:

• Wheat germ lipase
• immobilization
• esterification
• hydrolysis
• enzymatic resolution
• enzyme promiscuity

Disclosure statement

No potential conflict of interest was reported by the author(s).

Additional information

Funding

This work was supported by the National Science Centre, Poland, project OPUS No. 2016/B/ST5/03307.