This study was performd on 50 urine specimens of patients with type 2 diabetes, in addition, 50 normal specimens were investigated as control group. The activity rate of maltase in patients (6.40±2.17) I.U/ml and activity rate of maltase in normal (0.44±0.20)I.U/ml. The results of the study reveal that maltase activity of type 2 diabetes patient's urine shows significant increase (P<0.01) compare to normal.

Proteinases (E.C.3.4.21) family are widely distributed in the nature; it was present in animals tissues , plants and microbial cell . Protease was purified from Zahdi seed (Phoenix dactylifera L.) by several steps included ammonium sulphite ppt (75%) saturation and dialyzed against the 80mM sodium phosphate buffer at pH 7.5 . The enzyme specific activity was 407.62 unit/mg protein. The obtained extract was purified by DEAE-Cellulose column followed by gel filtration through Sephacyl S-200 column .The enzyme specific activity ,yield and purification fold were 1873.49 unit/mg protein, 22.99 and 58.42% respectively. The results of protease characterization showed that the molecular weight was 25118 daltons as determined by gel f

Beta-lactamase was purified from local isolate Klebsiella pneumonia by several steps included precipitation with ammonium sulphate at 20-40% saturation, DEAE- ion exchange chromatography and gel filtration on Sephacryl S-200 column. The obtained purification fold and recovery were 32.66; 47.04% respectively. The characterization of the purified beta-lactamase showed that the molecular weight was about 4000 daltons as determined by gel filtration.Purified enzyme had an optimal pH of 7 for activity and an optimal stability between pH 6.5-7.5, results shows that the optimal temperature appear to be 35 ? C .During storage the enzyme retained 72% at -20 ? C and retained 25% of the activity at the same period at 4 ? C.

Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.

  Seven [35%] and five [25%] Serratia marcescens  isolates were obtained out of 20 samples of lettuce and 20 samples of spinach, respectively, taken from different locations in a farm in Baghdad city. The isolate that produced chitinase in higher level was chosen to purify chitinase through several stages of purification including: ammonium sulfate precipitation, DEAE- sephadex ion exchange chromatograpgy and sephadex G-200 gel filtration with 89.5- fold purification and 30% recovery.       The purified chitinase was characterized and the molecular weight of enzyme was 59000 daltons by using gel filtration chromatography. The optimum pH and temperature of the purified chitinase were 6.0 and 50°

Bacteriocins were partially purified by ammonium sulphate 50% concentraction, bacteriocin activity of Pediococcus acidilactici-FMAC278 was 25600 U/ml with 5.8 folds and 7.6% yeild, the activity decrease to 12800 U/ml after dialysis with 6.3 folds and 3% yield, On the other hand the bacteriocin activity of Weissella paramesenteroides-DFR6 was 12800 U/ml with 2.7 folds and 8.8% yeild, after dialysis the activity became 6400 U/ml with 5.1 fold and 3.4% yield, Chicken Sausage were made by adding 0.25, 0.5 and 1% particaly purified bacteriocin to study its effect on microorganisms and increasing shelf life of Sausage. It is found that bacterial numbers were decreased after 3 days of storage at refrigerator at 0.5% conc. While the molds decrea