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. 2021 Apr 9;11:53. doi: 10.1186/s13568-021-01215-7

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© The Author(s) 2021, corrected publication 2021

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 6 — Multiple amino-acid sequence alignment of the serratiopeptidase from S. marcescens AD-W2, PRZN_SERME serralysin from S. marcescens (E-15) with 100% sequence identity, PRZN_SERMA Serralysin from S. marcescens with 98.6% sequence identity, 0A240AD01_SERFI Serralysin from S. ficaria with 92.6% sequence identity, D4E064_SEROD Serralysin from S. odorifera DSM 4582 with 82.8% sequence identity and E0SC28_DICD3 Secreted protease A from Dickeya dadantii with 64.8% sequence identity. The protein sequence from serratiopeptidase was aligned to see the similarities, differences, and conservation of various amino acid residues using multiple sequence alignment. The alignment was carried out by using Clustal W platform in Seaview software