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Characteristics of Raw Starch-Digesting α-Amylase of Streptomyces badius DB-1 with Transglycosylation Activity and Its Applications

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Abstract

Streptomyces badius DB-1 produces α-amylase extracellularly, and its production was enhanced 5.1-fold (from 9.47 ± 0.51 to 48.23 ± 1.45 U mL−1) due to optimization by one-variable-at-a-time and statistical approaches. Soluble starch emerged as the most influential factor that strongly affected enzyme production. The purified enzyme is a monomer with a molecular mass of ~57 kDa and optimally active at 50 °C and pH 6.0. The enzyme hydrolyzes soluble as well as raw starches into simpler sugars with a high proportion (>40.0 %) of maltotetraose. It is optimally active at moderate temperature and generates maltooligosaccharides from starch, thus, useful as an antistale in bread making. It also plays a role in increasing the formation of maltooligosaccharides due to transglycosylation activity, thus, finds application in functional foods. This is the first report on the production of raw starch-digesting α-amylase by S. badius with transglycosylation activity.

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Acknowledgments

The authors gratefully acknowledge financial assistance from the Department of Biotechnology and University Grants Commission, Government of India, New Delhi while carrying out the work presented in the manuscript. The authors thank Dr. Debananda Ningthoujam, Department of Biochemistry, Manipur University, Imphal (India) for providing actinobacterial cultures. The authors wish to thank Mr. Vijay Kumar Gupta (Tushar Nutritive Food Industry, New Delhi) for extending help in assessing the applicability of amylase in bread making.

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  1. Department of Microbiology, University of Delhi South Campus, Benito Juarez Road, New Delhi, 110021, India

    L. Shivlata & T. Satyanarayana

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Correspondence to T. Satyanarayana.

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Shivlata, L., Satyanarayana, T. Characteristics of Raw Starch-Digesting α-Amylase of Streptomyces badius DB-1 with Transglycosylation Activity and Its Applications. Appl Biochem Biotechnol 181, 1283–1303 (2017). https://doi.org/10.1007/s12010-016-2284-4

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