Abstract
A new thermostable α-amylase from Rhizopus oryzae FSIS4 was purified for first time and recovered in a single step using a three-phase partitioning (TPP) system. The fungal α-amylase, at a concentration of 1.936 U per kg of flour, was used in bread-making and compared to the commercial enzyme. The results showed a significant effect of the recovered α-amylase in the prepared bread and allowed us to improve the quality of the bread. The study indicated clearly that the recovered α-amylase is a potential candidate for future applications in the bread-making industry and in other food biotechnology applications.
Highlights
Alpha-amylase (1,4-α-D-glucanglucanohydrolase, EC 3.2.1.1) is the most important carbohydrate-degrading enzyme for starch-based industries [1]
The fungal strain R. oryzae FSIS4 (GenBank Accession No KU726976.1) isolated from the wheat seed cultivated in an arid area from Algerian Sahara [9] was propagated on Potato Dextrose Agar (PDA) medium plate at 40 ◦ C
The performance of the enzyme preparation from R. oryzae FSIS4 was tested in the bread making process using wheat flour with a relative humidity of
Summary
Alpha-amylase (1,4-α-D-glucanglucanohydrolase, EC 3.2.1.1) is the most important carbohydrate-degrading enzyme for starch-based industries [1]. Fungal α-amylases were considered as very safe additives [3] They may increase the level of fermentable sugars in the dough, promoting the fermentation of yeast and the formation of Maillard reaction products, which, in turn, intensify bread flavor and crust color [3]. Aqueous systems such as three-phase partitioning (TPP), known as simple, economical and quick methods, were described for the recovery of enzymes [4,5,6] This elegant non-chromatographic tool may be performed in a purification process to be used successfully in food industries [4], namely to provide amylases for baking industries. The performance of the enzyme preparation from R. oryzae FSIS4 was tested in the bread-making process and compared to a currently commercialized amylase
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