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Purification and Characterization of an Extracellular Low Temperature-Active and Alkaline Stable Peptidase from Psychrotrophic Acinetobacter sp. MN 12 MTCC (10786)

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Abstract

An extracellular low temperature-active alkaline stable peptidase from Acinetobacter sp. MN 12 was purified to homogeneity with a purification fold of 9.8. The enzyme exhibited specific activity of 6,540 U/mg protein, with an apparent molecular weight of 35 kDa. The purified enzyme was active over broad range of temperature from 4 to 60 °C with optimum activity at 40 °C. The enzyme retained more than 75 % of activity over a broad range of pH (7.0–11.0) with optimum activity at pH 9.0. The purified peptidase was strongly inhibited by phenylmethylsulfonyl fluoride, giving an indication of serine type. The K m and V max for casein and gelatin were 0.3529, 2.03 mg/ml and 294.11, 384.61 μg/ml/min respectively. The peptidase was compatible with surfactants, oxidizing agents and commercial detergents, and effectively removed dried blood stains on cotton fabrics at low temperature ranging from 15 to 35 °C.

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Acknowledgments

The authors are thankful to the Director, CSIR-Institute of Himalayan Bioresource Technology (IHBT), Palampur, for support and encouragement during the course of this investigation. The financial support received from the CSIR under NWP006 and award of Senior Research Fellowship to Richa Salwan is gratefully acknowledged. This is IHBT Publication Number: 2053.

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Correspondence to Ramesh Chand Kasana.

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Salwan, R., Kasana, R.C. Purification and Characterization of an Extracellular Low Temperature-Active and Alkaline Stable Peptidase from Psychrotrophic Acinetobacter sp. MN 12 MTCC (10786). Indian J Microbiol 53, 63–69 (2013). https://doi.org/10.1007/s12088-012-0344-1

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