| Autor: |
E. Selvarajan, Anbazagan Nivetha, Vaithilingam Mohanasrinivasan, Chandrasekaran Subathra Devi |
| Rok vydání: |
2019 |
| Předmět: |
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| Zdroj: |
Nanoscience and Biotechnology for Environmental Applications ISBN: 9783319979212 |
| DOI: |
10.1007/978-3-319-97922-9_7 |
| Popis: |
It is estimated that over 70% of the world’s adult population have problems in digesting lactose resulting from absent or reduced β-galactosidase activity in the small intestine. Estimates of the number of Americans affected by lactose intolerance (LI) range between 30 and 50 million, whereas approximately 75 million Americans are lactose maldigesters. Maldigestion is also a common occurrence in adults who have low-intestinal lactase activity. Lactose that is not digested transits to the lower small intestine and large intestine, thus creating the potential for symptoms. β-Galactosidase is one of the relatively few enzymes that have been used in large-scale processes to perform lactose hydrolysis and galacto-oligosaccharide production. Immobilization is the limitation of movement of biocatalysts according to chemical or physical treatment. Immobilized molecules technique using biomaterials and nano-biotechnology is a very interesting topic that is touching almost all aspects of our life. This review outlines information regarding lactose intolerance, overview of β-galactosidase and recent advances of nanoimmobilization on β-galactosidase to study lactose hydrolysis potential. The plausible advantages with their use include their (1) biocatalyst efficiency, (2) specific surface area, (3) mass transfer resistance and (4) effective enzyme loading. Enzyme immobilization is a usual requirement as a solution to obtain reusable biocatalysts and thus decrease the price of the expensive biocatalysts. Various immobilization methods have been developed, and in particular, specific attachment of enzymes on metal oxides such as ZnO has been an important focus of attention. The method of immobilization has an effect on the preservation of the enzyme structure and retention of the native biological function of the enzyme. Enzymes immobilized onto nanoparticles showed a broader working pH and temperature range and higher thermal stability than the native enzymes. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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