Accepted_test
Currently, enzyme preparations that hydrolyze starch, which constitutes a significant proportion of carbohydrates in the feed weight but has a low percentage of digestibility, are in demand in agriculture to increase the nutritional value of feed. Alpha-amylase (α-1,4-glucan-4-glucanohydrolase) is an endoamylase and catalyzes the hydrolysis of α-1,4-glycosidic bonds within the chain of starch and related carbohydrates to form substances with a low degree of polymerization such as glucose, maltodextrin, and oligosaccharides of various lengths. Research in the field of α-amylase production is related to the search for strains of highly efficient thermostable enzymes, improvement of various characteristics of synthesis, secretion of recombinant proteins, protection against protease degradation, etc., as well as the search for inexpensive substrates for industrial cultivation of strain-producers. α-amylases from bacteria of Bacillus subtilis, B. amyloliquefaciens, B. licheniformis, and B. stearothermophilus species are of industrial importance. Expression systems based on bacteria including B. subtilis and Brevibacillus choshinensis, the fungus Aspergillus oryzae and the yeast Pichia pastoris (Komagataella phaffii) have been used to produce recombinant α-amylases. The aim of the present work was the qualitative identification and relative quantification of the alpha-amylase enzyme derived from the genome of the yeast Komagataella phaffii.