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A Review on Psychrophilic β-D-Galactosidases and Their Potential Applications

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Abstract

The majority of the Earth’s ecosystem is frigid and frozen, which permits a vast range of microbial life forms to thrive by triggering physiological responses that allow them to survive in cold and frozen settings. The apparent biotechnology value of these cold-adapted enzymes has been targeted. Enzymes’ market size was around USD 6.3 billion in 2017 and will witness growth at around 6.8% CAGR up to 2024 owing to shifting consumer preferences towards packaged and processed foods due to the rising awareness pertaining to food safety and security reported by Global Market Insights (Report ID-GMI 743). Various firms are looking for innovative psychrophilic enzymes in order to construct more effective biochemical pathways with shorter reaction times, use less energy, and are ecologically acceptable. D-Galactosidase catalyzes the hydrolysis of the glycosidic oxygen link between the terminal non-reducing D-galactoside unit and the glycoside molecule. At refrigerated temperature, the stable structure of psychrophile enzymes adjusts for the reduced kinetic energy. It may be beneficial in a wide variety of activities such as pasteurization of food, conversion of biomass, biological role of biomolecules, ambient biosensors, and phytoremediation. Recently, psychrophile enzymes are also used in claning the contact lens. β-D-Galactosidases have been identified and extracted from yeasts, fungi, bacteria, and plants. Conventional (hydrolyzing activity) and nonconventional (non-hydrolytic activity) applications are available for these enzymes due to its transgalactosylation activity which produce high value-added oligosaccharides. This review content will offer new perspectives on cold-active β-galactosidases, their source, structure, stability, and application.

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Acknowledgements

The authors are thankful to the Head, Department of Biochemistry, Yogi Vemana University, Kadapa, for providing computation and other facilities to complete this article. R. Chikati sincerely thank the University Grant Commission (UGC), New Delhi (Lr. No. F 11-48/2008 (BSR), dated 12-02-2010) for financial support and also the D.S. Kothari Post Doctoral Fellowship (No. F. 4-2/06 (BSR)/BL/13-14/0228; dated 02/12/13). SLP gratefully acknowledges DBT (BT/PR30629/BIC/101/1093/2018), New Delhi; UGC (Ref No.: No. F. 30-456/2018 (BSR) and SERB (Ref No.: PDF/2015/000867) for the financial support.

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Authors and Affiliations

  1. Department of Biotechnology, Loyola Academy Degree & PG College, Old Alwal, 500010, Secunderabad, TS, India

    L. Joji Reddy & P. Suresh Kumar

  2. Onco-Stem Cell Research Laboratory, Department of Biochemistry and Bioinformatics, GITAM Institute of Science, GITAM Deemed to Be University, Visakhapatnam, 530045, India

    Santhi Latha Pandrangi

  3. Department of Biochemistry, Yogivemana University, Kadapa, 516005, AP, India

    Rajashekar Chikati & Ramachandra Reddy Pamuru

  4. Regional Ayurveda Research Institute, Itanagar, Arunachal Pradesh, India

    C. Srinivasulu

  5. Institute of Oceanography and Maritime Studies (INOCEM), Kulliyyah of Science, International Islamic University Malaysia, Kuantan, 25200, Pahang, Malaysia

    Akbar John

  6. Department of Agrotechnology, Faculty of Agro Based Industry (FIAT), Universiti Malaysia Kelantan, 17600, Jeli, Kelantan, Malaysia

    Arifullah Mohammed

  7. Vikrama Simhapuri University, Nellore, 524320, AP, India

    Ramachandra Reddy Pamuru

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  1. L. Joji Reddy
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  4. Rajashekar Chikati
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  5. C. Srinivasulu
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  8. Ramachandra Reddy Pamuru
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Contributions

Collection of literature and drafting the manuscript: LJR and PSK; conceptualized the study: LJR and RSC; computational validation of data and its reliability check: CRS; overall supervision of the study: PRC; validation and final preparation of the manuscript: PRC and AM.

Corresponding authors

Correspondence to Rajashekar Chikati, Arifullah Mohammed or Ramachandra Reddy Pamuru.

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Reddy, L.J., Kumar, P.S., Pandrangi, S.L. et al. A Review on Psychrophilic β-D-Galactosidases and Their Potential Applications. Appl Biochem Biotechnol 195, 2743–2766 (2023). https://doi.org/10.1007/s12010-022-04215-w

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