An uncharacterized protein from the metagenome with no obvious homology to known lipases shows excellent alkaline lipase properties and potential applications in the detergent industry.

Yue Xiao,Run-Qian Mao,Ge Yuan,Yi-De Liu,Gang Li

doi:10.1007/s10529-021-03203-0

Yue Xiao, Run-Qian Mao + Show 3 more

Open Access

https://doi.org/10.1007/s10529-021-03203-0

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Abstract

A novel lipase, Lip486, which has no obvious homology with known lipases, was discovered using functional metagenomics technology. Phylogenetic tree analysis suggested that the enzyme belongs to a new subfamily called lipolytic enzyme family II. To explore the enzymatic properties, lip486 was expressed heterologously and efficiently in Escherichia coli. The recombinant enzyme displayed the highest activity on the substrate p-nitrophenyl caprate with a carbon chain length of 10, and its optimum temperature and pH were 53°C and 8.0, respectively. The recombinant Lip486 showed good activity and stability in strong alkaline and medium-low-temperature environments. The results of compatibility and soaking tests showed that the enzyme had good compatibility with 4 kinds of commercial detergents, and an appropriate soaking time could further improve the enzyme activity. Oil stain removal test results for a cotton cloth indicated that the washing performance of commercial laundry detergent supplemented with Lip486 was further improved. In addition, as one of the smallest lipases found to date, Lip486 also has the advantages of high yield, good stability and easy molecular modification. These characteristics reflect the good application prospects for Lip486 in the detergent and other industries in the future.

Highlights

Lipase (EC3.1.1.3) is a special type of ester bond hydrolase that can catalyze the hydrolysis of triacylglycerides and decompose various natural oils and fats produced by organisms
A novel lipase, Lip[486], which has no obvious homology with known lipases, was discovered using functional metagenomics technology
The results showed that Lip[486] had the highest hydrolysis activity on the C10 substrate p-nitrophenyl caprate, and its hydrolysis activity on substrates with a carbon chain length greater than 10 was significantly higher than that on substrates with a carbon chain length below 10, indicating that Lip[486] is a lipase of esterases

Summary

Introduction

Lipase (EC3.1.1.3) is a special type of ester bond hydrolase that can catalyze the hydrolysis of triacylglycerides and decompose various natural oils and fats produced by organisms. Lipase acts as a catalyst at the oil-water interface and can catalyze transesterification, synthesis, hydrolysis and ammonolysis reactions in the nonaquesous phase (Casas-Godoy et al 2012), which has great research and development value, rendering lipase the third most important industrial enzyme after protease and glycosyl hydrolase (Martínez-Ruiz et al 2018). Lipases derived from microorganisms have more biodiversity than those from animals and plants. These lipases have many types and a wider operating temperature range, and the stability and activity of microbial lipases are higher. Lipase has a wide range of industrial applications, including food, washing, papermaking, environmental management, bioenergy, cosmetics, oil processing and other fields (Bharathi and Rajalakshmi 2019; Navvabi et al 2018; Priyanka et al 2019)

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