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We have synthesized Cu(II) complexes with m-hydroxy benzaldehyde semicarbazone (L1 =Hm-HBSC), m-hydroxy benzaldehyde thiosemicarbazone (L2= Hm-HBTSC), p-hydroxyl benzaldehyde semicarbazone (L3= Hp-HBSC) and p-hydroxybenzaldehyde thiosemicarbazone (L4= Hp-HBTSC). These complexes were characterized through elemental analysis, molecular weight, electrical conductance and magnetic susceptibilities at room temperature .The observed magnetic moments of all these complexes are consistent with the presence of a single unpaired electron. On the basis of above observations the complexes were proposed to be octahedral structure. These complexes were screened for anti-bacterial and antifungal properties and have exhibited potential activity.

A pH tolerant and thermostable protease inhibitor BTPI-301 active against trypsin was purified and characterized from P. mendocina that could be developed and used as biopreservative as well as biocontrol agent.

Protease inhibitors can be versatile tools mainly in the fields of medicine, agriculture and food preservative applications. Fungi have been recognized as sources of protease inhibitors, although there are only few such reports on mushrooms. This work reports the purification and characterization of a trypsin inhibitor from the fruiting body of edible mushroom Pleurotus floridanus (PfTI) and its effect on the activity of microbial proteases. The protease inhibitor was purified up to 35-fold by DEAE-Sepharose ion exchange column, trypsin-Sepharose column and Sephadex G100 column. The isoelectric point of the inhibitor was 4.4, and its molecular mass was calculated as 37 kDa by SDS-PAGE and 38.3 kDa by MALDI-TOF. Inhibitory activity confirmation was by dot-blot analysis and zymographic activity staining. The specificity of the inhibitor toward trypsin was with Ki of 1.043 × 10(-10) M. The inhibitor was thermostable up to 90 °C with maximal stability at 30 °C, active over a pH range of 4-10 against proteases from Aspergillus oryzae, Bacillus licheniformis, Bacillus sp. and Bacillus amyloliquefaciens. Results indicate the possibility of utilization of protease inhibitor from P. floridanus against serine proteases.

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