Dissertation
Dissertation > Agricultural Sciences > Gardening > Fruit trees gardening > Berries > Figs

Purification and Characterization of Ficin

Author HuangLu
Tutor WangXiaoPing
School Jilin University
Course Biochemistry and Molecular Biology
Keywords Fig tree gum Protease Separation and purification Characterization
CLC S663.3
Type Master's thesis
Year 2007
Downloads 286
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Ficin (EC 3.4.22.3) is a proteolytic enzyme is mainly present in the fig tree gum . Figs belong to the Moraceae Ficus plants . Ficin is a general term for a series of complex enzyme , these enzymes are single-chain thiol protease molecular weight of about 25,000 , and its enzymatic properties similar to papain . The ficin used the meat tenderizer agent, the wine industry in the food industry clarifying agents and stabilizers , surface point improver; production of protein hydrolyzate ; soft wool epidermis leather and textile industries ; medicine repellents ; enzymatic synthesis of peptides , ficin omnipotent catalyst . Fig tree gum compared to the high content of fruit protease and easy storage and transport , and therefore for the further development of the application of ficin , Shandong fig tree gum (Brunswike, country of origin , France Ficus carica) as raw material , the use of cation exchange and gel filtration chromatography separation and purification to obtain a ficin . Determined by SDS-PAGE and cathodic electrodeposition which is a single-chain protein , molecular weight of about 25kDa , vitality staining results determine protease . Enzyme most suitable for a catalyst temperature of 65 ℃, catalytic casein has two optimum pH , 7.0 and 9.0 , respectively . Heavy metal ions Cu 2 Zn 2 , Hg 2 completely inhibited the vitality , DTT, β -ME , L-Cysteine ??vitality activation . Enzyme at 65 ℃ half - life of greater than 1 hour , 75 ° C half-life of less than 20 minutes . 37 ° C under pH7.0 the enzyme casein hydrolyzate Km the value 1.56mg/mL . L-cysteine- activated enzyme the most suitable concentration for the 10- 20mmol / L . Contains two molecules of free sulfhydryl groups per molecule of enzyme . Enzyme a maximum absorption wavelength at 280nm . L-cysteine ??and the enzyme , fluorescence spectroscopy and circular dichroism change the native conformation of the enzyme .

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