| Grant number: | 19/23014-3 |
| Support Opportunities: | Research Grants - Innovative Research in Small Business - PIPE |
| Start date: | September 01, 2020 |
| End date: | May 31, 2021 |
| Field of knowledge: | Biological Sciences - Microbiology - Applied Microbiology |
| Principal Investigator: | Elisângela Soares Gomes Pepe |
| Grantee: | Elisângela Soares Gomes Pepe |
| Company: | Elisangela Soares Gomes Pepe |
| CNAE: |
Preparação do leite Fabricação de laticínios |
| City: | Jaboticabal |
| Pesquisadores principais: | Eliana Gertrudes de Macedo Lemos |
| Associated researchers: | Tereza Cristina Luque Castellane |
| Associated scholarship(s): | 20/10405-1 - Heterologous expression and initial characterization of one arabinose isomerase,
BP.TT 20/09892-5 - Development and determination of enzyme cocktail efficacy for low calorie zero lactose milk production, BP.PIPE |
Abstract
The richness of microbial enzymatic activities reflects a high number of metabolites derived from biotechnological application by the biorefinery of high-value-added foods. As an example, the ß-glucosidase enzyme promotes the release of flavouring agents due to its hydrolytic activity on Glycoside conjugates, which is widely applied in the production of wines and juices aiming at the release of flavouring compounds from of precursors such as Linalool, Geraniol and Nerol. However, the application of ²-glucosidases could be extended to modify sugars in other food products, exploring for example their "promiscuous" function as lactase, i.e., hydrolysis of lactose in glucose and galactose. Lactase activity is important for the food market with low lactose content, because half of the world's population suffers from malabsorption or lactose intolerance. Usually these processes make use of ²-galactosidases as lactases, however these enzymes are usually inhibited by their products (glucose) which limits their performance. Recently we published a study using the Bg10-tolerant/glucose-stimulated ß-glucosidase, capable of hydrolysing 55% of lactose in milk samples at 15 hours under low temperature (6 ° C), while it was able for hydrolysing almost 100% of lactose purified at only one hour under its optimum temperature (37 ° C), demonstrating a wide margin of optimization for process development under mild temperature conditions, allowing the maintenance of organoleptic properties of the product. Another biotechnological strand that might help the production of food beneficial to health is the exploration of enzymatic conversion pathways of common sugars in rare sugars such as tagatose and psicose, which are recognized for their sweetening properties of low calorie. The main obstacle to the full exploitation of rare sugars is the fact that these are found in a scarce way in nature, while having complex and high-costly chemical syntheses. The enzymatic conversion becomes, therefore, a highly viable option to enjoy the benefits of these products in a safe and effective way, since the enzymatic specificity prevents the formation of unwanted collateral products, such as the case of racemic mixtures that usually comes from chemical synthesis. Milk Zero Lactose is a well-consolidated biotechnological product in the food market, consumed not only by those who have lactose intolerance, but attractive for people seeking a low-caloric food, holding lower fat content. However, unlike the common sense of many consumers, the product does not have a "low carb" characteristic, since lactose in the product is hydrolysed into common sugars such as glucose and galactose, which are readily absorbed during the metabolism of food. Considering this opportunity to improve the products available to the customer, this project proposes not only to use the non-conventional system of hydrolysis of lactose by ß-glucosidase, but also to reduce the amount of calories of the product through the enzymatic conversion of half of carbohydrates from lactose hydrolysis into a natural rare type of food safety recognized as low absorbable by the human body: tagatose, converted from galactose by action of one isomerase. (AU)
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