PJB-2021-462
Comparative analysis of raw starch degradation using Aspergillus tubingensis SY 1
Saira Yahya
Abstract
Aim: Starchy biomass has paved its way in various applications because of its versatility and low cost. The study was designed to characterize cereal, and halophytic starches, the effect of a fungal amylase on these starches, and the utilization of these starches as a source for amylase production. Methods and Results: The cereal and halophytic starches were extracted and characterized on the basis of their hydration capacity, moisture content and pH. They were then subjected to fermentation by the fungal strain A. tubingensis SY 1. Maximum amylase yields (4.3 IU/ml, 72 hr.) under submerged fermentation (SmF) were obtained by the utilization of potato peels followed by barley bran (3.1 IU/ml, 80 hr.). In solid-state fermentation (SSF), maximum amylase production was observed using potato peels (17.8 IU/ml, 120 hr.) and wheat bran (10.7 IU/ml, 120 hr.). A wide range of substrate specificity was observed with the A. tubingensis SY 1 amylase, i.e., the ability to hydrolyze α-1,6 along with the α-1,4 glycosidic bonds. Strong amylase adsorption was observed in barley-bran, wheat-bran, and Phragmites karka stem among all the natural plant substrates used. For the scanning electron microscopy, substrates were hydrolyzed by Aspergillus tubingensis SY 1 amylase for 24 h which indicated that the enzyme is substrate-specific in action. Conclusions: Aspergillus tubingensis SY 1 produced substantial amounts of amylase under both solid-state (SSF) and submerged (SmF) fermentation conditions by consuming natural carbon sources, mainly barley-bran, wheat-bran, potato-peels, and the halophytes Phragmites karka and Typha domingensis. Significance and impact of the study: Potato peels, wheat bran and halophytes, Typha domingensis and Phargmites karka can prove prospective substrates for enzymatic production of amylases. Thus far, no study has shown the possible production of amylase from these halophytic plants, making them cheap and novel substrates for amylase production.
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