Stereoselectivity, a distinctive characteristic of lipase (EC 3.1.1.3), refers to the ability to differentiate between enantiomeric positions (sn-1 and sn-3) in triacylglycerol (TAG). This property has been determined based on the time course of enantiomeric excess of diacylglycerol (DAG) considering several consecutive steps of lipase-catalyzed hydrolysis of TAG; however, this concept is insufficient to represent the true nature of lipases which are capable of hydrolyzing the sn-2 position of TAG under the condition acyl migration occurs. Here, we suggest “integral stereoselectivity” to capture the preference of lipases for all ester groups of both TAG and DAG, as a novel index of the stereochemistry of lipase. To determine integral stereoselectivity, we established an analytical system based on the chromatographic resolution of dioleoylglycerol (DO) enantiomers and regioisomers. DO enantiomers were derivatized with 4-nitrophenyl isocyanate, and subsequently, resolved by chiral-phase high-performance liquid chromatography–ultraviolet. Regioisomers of monooleoylglycerol and DO were analyzed by HPLC with an evaporative light-scattering detector. Time-course analysis of three model lipases involved in the hydrolysis of trioleoylglycerol validated the analytical system designed to determine the integral stereoselectivity. As an accurate indicator of lipase stereochemistry reflecting all hydrolysis steps, integral stereoselectivity can expedite the development of lipases with unique stereochemistry from agricultural sources and their application to the food industry.

The objective of this study was to investigate the influence of pH value on the in vitro digestibility of malic acid-treated corn starch in relation to its structural properties. Varying pH values (1.5–8.5) of 2 M malic acid solution were combined with corn starch in a forced-air oven at 130 °C for 12 h. Using Fourier-transform infrared spectroscopy (FT-IR), carbonyl groups were detected in malic acid-treated corn starch, indicating cross-linking through esterification. As the pH value of malic acid-treated corn starch decreased from 8.5 to 1.5, the resistant starch content increased from 18.2 to 74.8%. This was the result of an increased degree of substitution and was maintained after gelatinization. The granular structure of malic acid-treated corn starches was not destroyed, and the starches maintained birefringence. This malic acid-treated corn starch could be utilized in heat processed foods such as bread and cookies as well as in products with reduced calories.

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Contrary to other solid catalysts, enzymes facilitate more sophisticated chemical reactions because most enzymes specifically interact with substrates and release selective products. Lipases (triacylglycerol hydrolase, EC 3.1.1.3), which can catalyze the cleavage and formation of various acyl compounds, are one of the best examples of enzymes with a unique substrate selectivity. There are already several commercialized lipases that have become important tools for various lipid-related studies, although there is still a need to discover novel lipases with unique substrate selectivity to facilitate more innovative reactions in human applications such as household care, cosmetics, foods, and pharmaceuticals. In this mini-review, we focus on concisely demonstrating not only the general information of lipases but also their substate selectivities: typoselectivity, regioselectivity, and stereoselectivity. We highlight the essential studies on selective lipases in terms of enzymology. Furthermore, we introduce several examples of analysis methodology and experimental requirements to determine each selectivity of lipases. This work would stress the importance of integrating our understanding of lipase chemistry to make further advances in the relevant fields.