Lactose hydrolysis in milk using a commercial recombinant β-galactosidase (lactase) from Bifidobacterium bifidum
Abstract We have identified the most relevant properties of a commercial recombinant lactase from Bifidobacterium bifidum (RBBL, Saphera 2600 L) for milk hydrolysis, with a yeast neutral lactase (GODO-YNL2) being used for comparison. Both products were characterized according to their lactase and in...
| Autores: | , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2022 |
| País: | Brasil |
| Institución: | Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
| Repositorio: | Food Science and Technology (Campinas) |
| Idioma: | inglés |
| OAI Identifier: | oai:scielo:S0101-20612022000101382 |
| Acceso en línea: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101382 |
| Access Level: | acceso abierto |
| Palabra clave: | enzyme technology low-lactose milk bacterial recombinant lactase |
| Sumario: | Abstract We have identified the most relevant properties of a commercial recombinant lactase from Bifidobacterium bifidum (RBBL, Saphera 2600 L) for milk hydrolysis, with a yeast neutral lactase (GODO-YNL2) being used for comparison. Both products were characterized according to their lactase and invertase activities, protein profiles by sodium-dodecyl-sulfate-polyacrylamide-gel electrophoresis, and Kms for lactose. RBBL exhibited properties that permitted milk hydrolysis over a broader range of conditions than YNL: apparently, milk’s ionic composition was not an activity-limiting property, an optimum temperature range between 45 and 50 °C and a considerable activity at pH 4.5, which would permit lactose hydrolysis in acidic dairy products. Like YNL, the bacterial lactase retains a considerable activity under refrigeration (3-7 °C). To describe the lactose-hydrolysis time course, an empirical model was used in which the glucose obtained was expressed as a function of the standard activity per unit volume and the reaction time. This model proved adequate to describe the glucose-formation kinetics at 7 °C and 45 °C, up to a 95% hydrolysis and to facilitate calculation of the volumen-based enzyme dosage to obtain a certain degree of hydrolysis – a fundamental consideration in evaluating the costs of applying the enzyme |
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