The fermentation of food products is a transformation and preservation process in which different metabolites are generated, contributing to consumer health. In this sense, this systematic review aims to analyze the factors that guide the perception and preference for fermented foods. In addition, different perspectives are proposed based on the findings. The systematic search was carried out in four databases: Emerald Insight, Science Direct, Wiley Online Library, and Multidisciplinary Digital Publishing Institute. The keywords used were (Title/Abstract): fermented products, overall liking, purchase intention, expectations, emotions, interculturality, perception, and consumers. Ninety-two articles (n = 92) were selected and classified. The factors identified were (1) biological and physiological, (2) extrinsic product characteristics, (3) intrinsic product characteristics, (4) psychological, (5) situational, and (6) sociocultural. Intrinsic product characteristics were the most relevant, while the situational factors were the least studied. Our main contribution was a multidisciplinary approach to addressing the different factors in an integrated way, allowing a broader perspective of both products and consumers. This approach could help the reader understand consumer behavior and propose product improvements.

Lipases and esterases are biocatalysts used at the laboratory and industrial level. To obtain the maximum yield in a bioprocess, it is important to measure key variables, such as enzymatic activity. The conventional method for monitoring hydrolytic activity is to take out a sample from the bioreactor to be analyzed off-line at the laboratory. The disadvantage of this approach is the long time required to recover the information from the process, hindering the possibility to develop control systems. New strategies to monitor lipase/esterase activity are necessary. In this context and in the first approach, we proposed a lab-made sequential injection analysis system to analyze off-line samples from shake flasks. Lipase/esterase activity was determined using p-nitrophenyl butyrate as the substrate. The sequential injection analysis allowed us to measure the hydrolytic activity from a sample without dilution in a linear range from 0.05–1.60 U/mL, with the capability to reach sample dilutions up to 1000 times, a sampling frequency of five samples/h, with a kinetic reaction of 5 min and a relative standard deviation of 8.75%. The results are promising to monitor lipase/esterase activity in real time, in which optimization and control strategies can be designed.