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Transcriptomic and quantitative (q)PCR analyses revealed that these lysozymes were expressed at different levels in various venom glands. Of them, SbLyzc1\u20133 with signal peptides displayed significant transcriptions in the venom glands, implicating these lysozymes as venom constituents. Functional assays found that SbLyzc1 and SbLyzc2 showed antibacterial activity against\n                      <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                      and\n                      <jats:italic>Enterococcus faecalis<\/jats:italic>\n                      . Three lysozymes (SbLyzi, SbLyzc1 and SbLyzc3) suppressed thrombin\u2010induced fibrin clot formation, indicating anticoagulant activity, with SbLyzc1 exhibiting the greatest potency [half\u2010maximal inhibitory concentration (IC\n                      <jats:sub>50<\/jats:sub>\n                      )\u2009=\u20090.036\u2009\u00b1\u20090.003\u2009\u03bcg\u2009\u03bcL\n                      <jats:sup>\u20131<\/jats:sup>\n                      ]. SbLyzi and SbLyzc1 inhibited phenoloxidase activity in the hemolymph of the yellow mealworm\n                      <jats:italic>Tenebrio molitor<\/jats:italic>\n                      pupae, thereby suppressing its hemolymph melanization, with maximal inhibition rates of 78.4% and 74.3%, respectively. All four lysozymes exhibited insecticidal effects, causing &gt;80% mortality in yellow mealworm pupae following injection of 6\u2009\u03bcg per individual, with SbLyzc1 showing the highest insecticidal potency [half\u2010maximal lethal dose (LD\n                      <jats:sub>50<\/jats:sub>\n                      )\u2009=\u20094.25\u2009\u00b1\u20090.51\u2009\u03bcg\u2009g\n                      <jats:sup>\u20131<\/jats:sup>\n                      ].\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>CONCLUSION<\/jats:title>\n                    <jats:p>\n                      These findings demonstrate that lysozymes from\n                      <jats:italic>S.\u2009bifidus<\/jats:italic>\n                      possess multifunctional biological activities and SbLyzc1\u20133 act as significant venom components involved in capturing prey, providing new insights into the functional diversity of lysozymes in predatory bugs and their potential application in biological control strategies. \u00a9 2026 Society of Chemical Industry.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1002\/ps.71048","type":"journal-article","created":{"date-parts":[[2026,6,22]],"date-time":"2026-06-22T04:42:06Z","timestamp":1782103326000},"page":"10100-10110","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Multifunctional lysozymes from the assassin bug\n                    <scp>\n                      <i>Sycanus bifidus<\/i>\n                    <\/scp>\n                    : Insecticidal proteins with anticoagulant and melanization inhibition properties"],"prefix":"10.1002","volume":"82","author":[{"given":"Yuhan","family":"Liu","sequence":"first","affiliation":[{"name":"Key Laboratory of Forest Disaster Warning and Control of Yunnan Province Southwest Forestry University  Kunming 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