Abstarct: Cydia pomonella (L.) (Lep: Tortricidae) is one of the most important pests of apple orchards, which causes significant damage every year. Today, in order to control the harmful insects, much attention has been paid to their physiological characteristics, with the aim of disturbing the digestive processes and absorption of food in their stomachs. The determination of biochemical properties of digestive enzymes is the first effective step in the adoption of physiological control methods. To determine the physiology of digestion of apple grape, polluted apple fruits in spring and summer were collected from the Torbat Jam turtlenecks, and apple larvae were removed from the fruits and examined. The gastrointestinal tract of larvae of age 5 was extracted separately in laboratory conditions and stored for -20 freezing for enzymatic evaluation. The maximum activity of α-amylase, α-glucosidase and β-glucosidase enzymes was investigated in the presence of starch substrate, para-nitrophenyl α-glucopyranoside and para nitrophenyl β-glucopyranoside and in the range of different acidity and their optimum at pH 10, 8 and 8. The optimal temperature of these enzymes was tested at different temperature ranges, respectively at 35, 30 and 30 respectively. Using the azocasin substrate, the activity of the general protease of the gastrointestinal tract in a range of acidity was studied and it was determined that its maximum activity was at pH=11. The optimal temperature of the protease was also measured at 30 ° C. The activity of trypsin, chymotrypsin and elastase specific proteases was also studied by using special substrates of benzoyl-L-arginine-p-nitroallanidesuccinyl-Alanine-Alanine-Proline-phenylalanine-p nitroallanide , n-succinylalanine-alanine-alanine-p-nitroalanide were studied in a range of acidity and peak activity at pH=11. The optimal temperature of all three proteases was observed at 30 ° C. In addition, the acidity of the lipase enzyme with paranitrophenyl butyrate specific substrate was 8 and its maximum operating temperature was 40 ° C. In the study of concentrations of 5 and 10 mM ions Fe2+, Mg2+, Mn 2+, Mn2+, Zn2+ and Cu2+ copper on α- glucosidase and β-glucosidase enzymes, trypsin, chimotrypsin, elastase and lipase with specific substrates, 10 mM ion Cu2+ increased the enzymatic activity of α-glucosidase, β-glucosidase and other ions inhibited this enzyme activity and decreased activity. In studying the effect of different concentrations of the mentioned ions on serum protease activity, the activity of the enzyme elastase was increased by the effect of Zn2+ 5 mM and other ions reduced the serum protease activity. The lipase enzyme was also inhibited by these ions, and Cu2+ showed neutral state at both concentrations of 5 and 10 mM. The α-amylase zymograms showed two isoforms of this enzyme, as well as trypsin special protease zymograms using two band nitrocellulose plates in the C. pomonella (L.) gastrointestinal tract. The general protease zymogram was shown using a four band hemoglobin substrate.