Nanoimmobilization of β-Galactosidase for Lactose-Free Product Development

Selvarajan, Ethiraj; Nivetha, Anbazagan; Subathra Devi, Chandrasekaran; Mohanasrinivasan, Vaithilingam

doi:10.1007/978-3-319-97922-9_7

Ethiraj Selvarajan^8,9,
Anbazagan Nivetha⁸,
Chandrasekaran Subathra Devi⁸ &
…
Vaithilingam Mohanasrinivasan⁸

Part of the book series: Environmental Chemistry for a Sustainable World ((ECSW,volume 22))

1529 Accesses
2 Citations

Abstract

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.

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The authors are thankful to the Management, VIT University, Vellore, for providing the facilities and constant encouragement for this work.

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School of Bio Sciences & Technology, Vellore Institute of Technology, Vellore, Tamil Nadu, India
Ethiraj Selvarajan, Anbazagan Nivetha, Chandrasekaran Subathra Devi & Vaithilingam Mohanasrinivasan
Department of Genetic Engineering, School of Bioengineering, SRM Institute of Science & Technology, Kattankulathur, Chennai, Tamil Nadu, India
Ethiraj Selvarajan

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Ethiraj Selvarajan
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Anbazagan Nivetha
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Chandrasekaran Subathra Devi
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Correspondence to Vaithilingam Mohanasrinivasan .

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School of Bio Sciences & Technology, Vellore Institute of Technology, Vellore, Tamil Nadu, India
K M Gothandam
DST-Centre for Policy Research, Lucknow, Uttar Pradesh, India
Shivendu Ranjan
Department of Biotechnology, Institute of Engineering and Technology Dr. A.P.J. Abdul Kalam Technical University, Lucknow, Uttar Pradesh, India
Nandita Dasgupta
Aix-Marseille University, CEREGE, CNRS, IRD, INRA, Coll France, Aix en Provence, France
Eric Lichtfouse

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Ethical Approval This article does not contain any studies with human participants or animals performed by any of the authors.

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Selvarajan, E., Nivetha, A., Subathra Devi, C., Mohanasrinivasan, V. (2019). Nanoimmobilization of β-Galactosidase for Lactose-Free Product Development. In: Gothandam, K., Ranjan, S., Dasgupta, N., Lichtfouse, E. (eds) Nanoscience and Biotechnology for Environmental Applications. Environmental Chemistry for a Sustainable World, vol 22. Springer, Cham. https://doi.org/10.1007/978-3-319-97922-9_7

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DOI: https://doi.org/10.1007/978-3-319-97922-9_7
Published: 06 February 2019
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-97921-2
Online ISBN: 978-3-319-97922-9
eBook Packages: Earth and Environmental ScienceEarth and Environmental Science (R0)

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