생강으로부터 proteolytic protease를 직접 추출하고 정제하여 그 특성을 검토하였다. 생강을 마쇄하여 acetone으로 처리하여 얻은 filetr cake(여과박)를 건조시켜 acetone pow-der를 얻었다. Acetone powder로 부터 proteolytic protease의 성분을 추출하여 acetone 40~60% 분획과 DEAE-Sephacel ion exchange chromatography를 행하여 비효소활성이 42.9u/mg으로 15배이상 부분 정제되었다. 이 부분정제된 효소는 60℃, pH 6.0에서 각각 최고의 활성을 나타냈다. Fe+2철이온에 의해서 약 120~130% 활성화된 반면에 Cu+2, Ag+와 pCMB에 의한 현저한 활성저하를 보였고, cysteine 첨가시 무첨가에 비해 약 5배의 활성이 증가되었으며, 40℃에서 30분간 가열시 효소활성이 그대로 유지되었다.

Proteolytic protease of ginger was extracted from fresh ginger root and partially pur-ified and then its characteristics were studied. After grinding the ginger and extracting with acetone. Acetone powder was prepared by filtering the extract and drying the filter cake. Proteolytic protease was extracted from acetone powder and partially purified about 15folds by acetone fractionation 40~60% and DEAE-Sephacel ion exchange chromatography. Optimum pH and temperature were 6.0 and 60℃, respectively. The enzyme was acti-vated by Fe+2, Fe+3 ion and cysteine-HCI. The enzyme was fairly stable after incu-bation at 40℃ for 30 minutes.