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Jian Yang,Jie Li,Yunfeng Hu,Lizhen Li,Lijuan Long,Fazuo Wang,Si Zhang 한국생물공학회 2015 Biotechnology and Bioprocess Engineering Vol.20 No.1
High value utilization of byproduct of slaughterhousesis regarded as beneficial to both economy andenvironment. A hemoglobin degrading protease PA720was purified from fermentation broth of a Porites luteaassociated strain Streptomyces rutgersensis SCSIO 11720(SCSIO 11720) and exhibited maximal activity at 70°C,pH 10.5. The isolated strain was identified by genotypicmethod and 16 s RNA gene sequence was deposited inGenBank under accession No. KC414842. The enzymeexhibited excellent thermostability since it was stable at 70°Cwith t1/2 value of 1,386.3 min. Kinetic and thermodynamicstudy showed the activation energy (Ea), ΔG* (free energy),ΔH* (enthalpy) and ΔS* (entropy) for protease deactivationwere 62.71 kJ/mol, 74.26 kJ/mol, 59.86 kJ/mol, and-41.97 J/mol/K, respectively. Highest specific activity ofprotease PA720 was observed when using casein (9,953 U/mg)and hemoglobin (9,854 U/mg) as substrates. Hemoglobinhydrolysate prepared by protease PA720 showed significantantibacterial activity towards Escherichia coli, Staphylococcusaureus and Bacillus subtilis, indicating this protease couldbe used as an instrumental enzyme for production ofhemoglobin-based antibacterial peptides. Based on partialamino acid sequences of the enzyme PA720, the full geneencoding this protease was obtained by degenerate primerPCR and has been deposited in GenBank under accessionNo. KC414842. The deduced amino acid sequence exhibitshomology with other microbial thermophilic proteases insubtilisin family.
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