Abstract
L-asparaginase (E.C.3.5.1.1) hydrolyzes L-asparagine to L-aspartic acid and ammonia, which has been widely applied in the pharmaceutical and food industries. Microbes have advantages for L-asparaginase production, and there are several commercially available forms of L-asparaginase, all of which are derived from microbes. Generally, L-asparaginase has an optimum pH range of 5.0–9.0 and an optimum temperature of between 30 and 60 °C. However, the optimum temperature of L-asparaginase from hyperthermophilic archaea is considerable higher (between 85 and 100 °C). The native properties of the enzymes can be enhanced by using immobilization techniques. The stability and recyclability of immobilized enzymes makes them more suitable for food applications. This current work describes the classification, catalytic mechanism, production, purification, and immobilization of microbial L-asparaginase, focusing on its application as an effective reducer of acrylamide in fried potato products, bakery products, and coffee. This highlights the prospects of cost-effective L-asparaginase, thermostable L-asparaginase, and immobilized L-asparaginase as good candidates for food application in the future.
Highlights
Accepted: 2 August 2021L-asparaginase (L-asparagine amidohydrolase, E.C.3.5.1.1), which was first mentioned by Clementi in 1922, catalyzes the hydrolysis of L-asparagine into aspartic acid and ammonia (Figure 1A) [1,2,3]
Acrylaway® and PreventAse® are commercially available forms of L-asparaginase from fungi (Aspergillus oryzae and Aspergillus niger) [5,22], which are safe and are recommended for use as food additives by the FAO/WHO Expert committee [22,23]
L-asparaginase can effectively reduce the acrylamide content in food such as fried potato products, bakery products, and coffee, some aspects of its application still need to be further discussed
Summary
L-asparaginase (L-asparagine amidohydrolase, E.C.3.5.1.1), which was first mentioned by Clementi in 1922, catalyzes the hydrolysis of L-asparagine into aspartic acid and ammonia (Figure 1A) [1,2,3]. Acrylamide is formed between reducing sugars such as glucose and L-asparagine due to frying, baking, or grilling starchy foods at over 120 ◦ C in low humidity conditions through a non-enzymatic process called the Maillard reaction [10,11,12,13]. L-asparaginase is a promising choice because of its hydrolytic activity toward L-asparagine into aspartic acid and ammonia in the treatment of foods. Aspartic acid cannot participate in the Maillard reaction, meaning acrylamide formation is significantly inhibited (Figure 2B) [21]. Microbial sources of L-asparaginase are discussed: including classification, catalytic mechanism, production, purification and immobilization, focusing on its potential application for acrylamide mitigation in food such as fried potato products, bakery products, and coffee. L-asparaginase that make it more suitable for food application are addressed
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