Recombinant metalloprotease as a perspective enzyme for meat tenderization
eptidase family M9 (MEROPS database) is true collagenases and contains bacterial collagenases from Vibrio and Clostridium. One of the producers of M9A subfamily peptidase is Aeromonas salmonicida (locus - ASA_3723). The aim of the study was production of recombinant metallopeptidase Aeromonas salmon...
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| Format: | Article |
| Language: | English |
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HACCP Consulting
2019-08-01
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| Series: | Potravinarstvo |
| Subjects: | |
| Online Access: | https://potravinarstvo.com/journal1/index.php/potravinarstvo/article/view/1087 |
| _version_ | 1818823967854559232 |
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| author | Mikhail Minaev Anzhelika Aleksandrovna Makhova |
| author_facet | Mikhail Minaev Anzhelika Aleksandrovna Makhova |
| author_sort | Mikhail Minaev |
| collection | DOAJ |
| description | eptidase family M9 (MEROPS database) is true collagenases and contains bacterial collagenases from Vibrio and Clostridium. One of the producers of M9A subfamily peptidase is Aeromonas salmonicida (locus - ASA_3723). The aim of the study was production of recombinant metallopeptidase Aeromonas salmonicida by transformation Pichia pastoris for further meat tenderization. Laboratory amounts of recombinant peptidase were obtained and test evaluation of enzyme activity was performed. Recombinant peptidase broke the peptide bond «Pro-Leu-Gly-Met-Trp-Ser-Arg» (one of the collagen chains, (Mw = 846.06)). The concentration of the substrate (peptide) after 180 min was 2 – fold decrease as compared with control. The maximum shear force of heat-treated samples had a 1.27 – fold decrease as compared with the control. As a result of histological studies of beef shank samples, the specific effect of the supernatant on the structure of connective tissue was established. Muscle fibers have not changed. The recombinant enzyme could be used for the meat tenderization. |
| first_indexed | 2024-12-18T23:48:24Z |
| format | Article |
| id | doaj.art-a040140e635c48ffa5c1248dab6adb6a |
| institution | Directory Open Access Journal |
| issn | 1337-0960 |
| language | English |
| last_indexed | 2024-12-18T23:48:24Z |
| publishDate | 2019-08-01 |
| publisher | HACCP Consulting |
| record_format | Article |
| series | Potravinarstvo |
| spelling | doaj.art-a040140e635c48ffa5c1248dab6adb6a2022-12-21T20:47:08ZengHACCP ConsultingPotravinarstvo1337-09602019-08-0113162863310.5219/1087804Recombinant metalloprotease as a perspective enzyme for meat tenderizationMikhail Minaev0https://orcid.org/0000-0002-0038-9744Anzhelika Aleksandrovna Makhova1https://orcid.org/0000-0002-2508-2888V. M. Gorbatov Federal Research Center for Food Systems of Russian Academy of Sciences, Department of hygiene of production and microbiology, Talalikhina st. 26, 109316, Moscow, V.M. Gorbatov Federal Research Center for Food Systems of Russian Academy of Sciences, Department of hygiene of production and microbiology, Russia, Moscow, 26 Talalikhina st.eptidase family M9 (MEROPS database) is true collagenases and contains bacterial collagenases from Vibrio and Clostridium. One of the producers of M9A subfamily peptidase is Aeromonas salmonicida (locus - ASA_3723). The aim of the study was production of recombinant metallopeptidase Aeromonas salmonicida by transformation Pichia pastoris for further meat tenderization. Laboratory amounts of recombinant peptidase were obtained and test evaluation of enzyme activity was performed. Recombinant peptidase broke the peptide bond «Pro-Leu-Gly-Met-Trp-Ser-Arg» (one of the collagen chains, (Mw = 846.06)). The concentration of the substrate (peptide) after 180 min was 2 – fold decrease as compared with control. The maximum shear force of heat-treated samples had a 1.27 – fold decrease as compared with the control. As a result of histological studies of beef shank samples, the specific effect of the supernatant on the structure of connective tissue was established. Muscle fibers have not changed. The recombinant enzyme could be used for the meat tenderization.https://potravinarstvo.com/journal1/index.php/potravinarstvo/article/view/1087meat tenderizationrecombinant peptidasem9 family peptidase |
| spellingShingle | Mikhail Minaev Anzhelika Aleksandrovna Makhova Recombinant metalloprotease as a perspective enzyme for meat tenderization Potravinarstvo meat tenderization recombinant peptidase m9 family peptidase |
| title | Recombinant metalloprotease as a perspective enzyme for meat tenderization |
| title_full | Recombinant metalloprotease as a perspective enzyme for meat tenderization |
| title_fullStr | Recombinant metalloprotease as a perspective enzyme for meat tenderization |
| title_full_unstemmed | Recombinant metalloprotease as a perspective enzyme for meat tenderization |
| title_short | Recombinant metalloprotease as a perspective enzyme for meat tenderization |
| title_sort | recombinant metalloprotease as a perspective enzyme for meat tenderization |
| topic | meat tenderization recombinant peptidase m9 family peptidase |
| url | https://potravinarstvo.com/journal1/index.php/potravinarstvo/article/view/1087 |
| work_keys_str_mv | AT mikhailminaev recombinantmetalloproteaseasaperspectiveenzymeformeattenderization AT anzhelikaaleksandrovnamakhova recombinantmetalloproteaseasaperspectiveenzymeformeattenderization |