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Purification and Characterization of a Metalloprotease Produced by the C8 Isolate of Serratia Marcescens Using Silkworm Pupae or Casein as a Protein Source

Purification and Characterization of a Metalloprotease Produced by the C8 Isolate of Serratia Marcescens Using Silkworm Pupae or Casein as a Protein Source

Jenny Marcela Vélez-Gómez, Jhon Jairo Melchor-Moncada, Luz Angela Veloza, Juan Carlos Sepúlveda-Arias

Int J Biol Macromol. 2019 Aug 15;135:97-105.

PMID: 31125647

Abstract:

Serratiopeptidase, a metalloprotease produced by Serratia marcescens, is produced through a fermentation process using carbohydrates and proteins as carbon and nitrogen sources. However, some byproducts of the silk industry could be an alternative source for serratiopeptidase production. Therefore, the present work is focused on the purification and characterization of a serratiopeptidase produced from the C8 isolate of Serratia marcescens and obtained from a Colombian silkworm hybrid using casein or silkworm pupae. The protease was purified using ultrafiltration, anion-exchange, and size-exclusion chromatography. The purified enzyme showed a molecular weight of ~50 kDa with a purity above 96%, an isoelectric point of ~4.6, optimum pH and temperature of 6 and 50 °C, and stability at 4 °C for one month. The kinetic constants using azocasein as substrate were 0.63 mM (Km), 2,016 μM/min (Vmax), 41.41 s-1 (Kcat), and 6.56 × 107 M-1 s-1 (Kcat/Km). Inhibition by 5 mM EDTA or 1,10-phenanthroline was recovered by adding Zn2+ at the same concentration. Mass spectrometry analysis indicated 94% homology with the sequence of serratiopeptidase produced by the E-15 strain. We purified and characterized a serratiopeptidase produced by the C8 isolate of S. marcescens in a culture medium based on a renewable source from the silk industry.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP102110747	Azocasein		102110-74-7	Price

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