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Updates on naringinase: structural and biotechnological aspects

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Abstract

Naringinases has attracted a great deal of attention in recent years due to its hydrolytic activities which include the production of rhamnose, and prunin and debittering of citrus fruit juices. While this enzyme is widely distributed in fungi, its production from bacterial sources is less commonly known. Fungal naringinase are very important as they are used industrially in large amounts and have been extensively studied during the past decade. In this article, production of bacterial naringinase and potential biotechnological applications are discussed. Bacterial rhamnosidases are exotype enzymes that hydrolyse terminal non-reducing α-l-rhamnosyl groups from α-l-rhamnose containing polysaccharides and glycosides. Structurally, they are classified into family 78 of glycoside hydrolases and characterized by the presence of Asp567 and Glu841 in their active site. Optimization of fermentation conditions and enzyme engineering will allow the development of improved rhamnosidases for advancing suggested industrial applications.

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Acknowledgement

The author would like to thank Director, Centre for Biotechnology and Interdisciplinary Sciences (CBIS), ITRI for providing the necessary facility to carry out this work at Deakin University, Australia. Some of the data presented in this write-up has emanated from the research work carried at Department of Biotechnology, Punjabi University, India.

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The author declare that he has no conflict of interest.

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  1. Centre for Biotechnology, Chemistry and System Biology (Biodeakin), Institute of Technology Research and Innovation (ITRI), Deakin University, Warrnambool, Victoria, 3217, Australia

    Munish Puri

  2. Fermentation and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Punjab, India

    Munish Puri

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Puri, M. Updates on naringinase: structural and biotechnological aspects. Appl Microbiol Biotechnol 93, 49–60 (2012). https://doi.org/10.1007/s00253-011-3679-3

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