Lactate detection sensors for food, clinical and biological applications: a review

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Lactate detection sensors for food, clinical and biological applications: a review Gurdeep Rattu1 · Nishtha Khansili1 · Vaibhav Kumar Maurya1 · Prayaga M. Krishna1  Received: 22 June 2020 / Accepted: 1 October 2020 © Springer Nature Switzerland AG 2020

Abstract l-lactate is a major analyte in the food industry, bioprocess engineering, sports medicine and clinical care unit. l-lactate detection by standard analytical techniques is expensive, time-consuming and difficult for in situ studies. Therefore, selective l-lactate biosensors are developed to overcome the current challenges of food industries and biological sectors. High-throughput nanobiosensors appear promising for on-site detection of lactate in industrial- and laboratory-scale applications. Here, we review principles of lactate sensing techniques and trends in transduction approaches. We discuss nanomaterials, merits and demerits of enzyme-based lactate analysis and commercial testing kits. We present also non-enzymatic nanobiosensors. Keywords  l-Lactate · Enzymes · Food · Nanoparticles · Enzyme free · Biosensors

Introduction DL-Lactic acid, ­C3H6O3 or C ­ H3CHOHCOOH, is the racemic isomer of lactic acid also named 2-hydroxypropanoic acid. It is generally a non-volatile, odourless, colourless, crystalline substance and dissociates almost completely to lactate (Hosoya et al. 2001). It is referred as Generally Recognized as Safe by U.S. Food and Drug Administration (USFDA). This organic acid belongs to the family of alpha-hydroxy acids and it is present in the soil, certain plant juices, in the blood and muscles of animals (Jia et al. 2013; Teusink and Molenaar 2017). It is the prevalent acidic constituent of fermented milk and dairy products, sports medicine, bioprocess engineering and food manufacturing (Fig. 1) (Nikolaus and Strehlitz 2008; Dai et al. 2017). Lactic acid is the final product of sugar metabolism: it may undergo esterification with organic acids and oxygenation or dehydrogenation to form pyruvic acid or its derivatives (Kamel et al. 2019). This also results in production of nicotinamide adenine dinucleotide (NAD), that is used to produce adenosine triphosphate (ATP) in glycolysis. l -lactate has been a by-product of cellular metabolism * Prayaga M. Krishna [email protected] 1



Department of Basic and Applied Science, National Institute of Food Technology Entrepreneurship and Management (NIFTEM), Kundli, Haryana 131028, India

which indicates a transition from aerobic to anaerobic condition. Thus, anaerobic metabolism results in the production of l-lactate by the action of lactate dehydrogenase (LDH, lactate oxidizing enzyme) as an end product of glycolysis (Kamel et al. 2019). The two lactate isomers are known as l-lactate and d-lactate. In humans, the lactate produced is almost exclusively L-lactate. Blood contains approximately 100 times more l-lactate than d-lactate (Goodwin et al. 2007; Tuteja et al. 2018). Pathological significance of lactate is almost entirely confined to the l-lactate isoform and it is specific