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A novel maltooligosaccharide-forming α-amylase from Bacillus cereus and its application in the preparation of maltopentaose product.

Authors :
Pan, Shiyou
Wang, Guiping
Sun, Chang
Du, Liqin
Qi, Xianghui
Wei, Yutuo
Source :
Process Biochemistry. May2023, Vol. 128, p68-75. 8p.
Publication Year :
2023

Abstract

Maltooligosaccharides (MOS) have become a prominent market in the pharma and food industries due to their excellent bio-preservative and prebiotic properties. However, producing specific maltooligosaccharides like maltopentaose (G5) is relatively tedious and expensive. Here, a novel maltooligosaccharide-forming α-amylase from Bacillus cereus (BcMFAse) was characterized and exhibited a specific activity of 1965.0 ± 9.7 U/mg. The BcMFAse principally produced G5 by hydrolyzing soluble starch, with a maximum G5 yield of 215.8 ± 5.9 g/kg starch, accounting for 63.8 % of the saccharide mixture. The enzymatic hydrolysate was purified by AB-8 macroporous resin column chromatography. Briefly, 1.0 mL adsorbate containing 486.6 g/L total saccharides with deionized water elution at a flow rate of 0.7 mL/min and column temperature of 55 °C. Afterward, G5 was enriched up to 95.4 % purity, and 72.2 % was recovered in solution. The proposed process was simulated by SuperPro Designer software, and the remarkable economic results included a payback period of 0.08 years and an internal rate of return of 294.6 %. This study represented that BcMFAse could be a promising candidate for applications in the food and pharma fields. It first provided a high-efficiency process for producing > 90 % pure G5, which was economically attractive on an industrial scale. [Display omitted] • A novel maltooligosaccharide-forming α-amylase (BcMFAse) was firstly reported. • BcMFAse had 1965 U/mg of amylase activity and 63.8 % of maltopentaose specificity. • A high-efficiency process for producing pure maltopentaose was developed. • 95.4 % of maltopentaose purity was achieved by AB-8 macroporous resin purification. • Techno-economic analysis of high-purity maltopentaose production was conducted. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
13595113
Volume :
128
Database :
Academic Search Index
Journal :
Process Biochemistry
Publication Type :
Academic Journal
Accession number :
162705183
Full Text :
https://doi.org/10.1016/j.procbio.2023.02.016