α--AMYLASES OF Aspergillus flavus var. oryzae AND Bacillus subtilis: THE SUBSTRATE SPECIFICITY AND RESISTANCE TO A NUMBER OF CHEMICALLY ACTIVE SUBSTANCES

Biotechnologia Acta

卷:6

L. D. Varbanets¹  K. V. Avdiyuk¹ 

[1] Institute of Microbiology and Virology of National Academy of Sciences of Ukraine, Kiyv;

关键词: Aspergillus flavus var. oryzae;    Bacillus subtilis;    α-amylase;    substrate specificity;    Michaelis constant;   

DOI  :  10.15407/biotech6.03.036

来源: DOAJ

【 摘 要 】

The ability of Aspergillus flavus var. oryzae 80428 and Bacillus subtilis 147 α-amylases to split different carbohydrate-containing substrates, such as maltose, sucrose, trehalose, dextrin, α- and β-cyclodextrin, amylose, amylopectin, glycogen, pullulan, soluble starch, insoluble starch, corn starch, wheat starch, dextran 500has been studied. It was shown that investigated enzymes differ by substrate specificity. α-Amylase of A. flavus var. oryzae 80428 rapidly hydrolysed soluble potato and wheat starch, while the α-amylase of B. subtilis 147 — only wheat starch. Both enzymes don’t cleave maltose, α-cyclodextrin and dextran 500. A. flavus var. oryzae 80428 α-amylase display very small ability to hydrolyze pullulan, while α-amylase of B. subtilis 147 it does not act in general. The lowest values of Michaelis constant for both enzymes at splitting of glycogen have been obtained, indicating that enzymes have the greatest affinity to this substrate. The studies of influence of chemically active substances on activity of A. flavus var. oryzae 80428 and B. subtilis 147 ?-amylases show there are resistant to urea, deoxycholic acid, Tween-80, Triton X-100 and hydrogen peroxide. It’s indicate the enzymes tested may be competitive in compare with earlier described in literature enzymes. The obtained results give a possibility to propose in future usage these enzymes in different fields of industry, foremost in detergent industry.

【 授权许可】

Unknown