Search

The current research in the food industry regarding enzymatic modification to enhance the freeze-thaw (FT) stability of starch is limited. The present study aimed to investigate the FT stability of normal corn starch (NCS) modified using 1,4-α-glucan branching enzyme (GBE) derived from Geobacillus thermoglucosidans STB02. Comprehensive analyses, including syneresis, scanning electron microscopy, and low-field nuclear magnetic resonance, collectively demonstrated the enhanced FT stability of GBE-modified corn starch (GT-NCS-30) in comparison to its native form. Its syneresis was 66.4 % lower than that of NCS after three FT cycles. Notably, GBE treatment induced changes in the pasting properties and thermal resistance of corn starch, while simultaneously enhancing the mechanical strength of the starch gel. Moreover, X-ray diffractograms and microstructural assessments of freeze-thawed gels indicated that GBE treatment effectively hindered the association of corn starch molecules, particularly amylose retrogradation. The enhanced FT stability of GBE-modified starch can be attributed to alterations in the starch structure induced by GBE. This investigation establishes a foundation for further exploration into the influence of GBE treatment on the FT stability of starch and provides a theoretical basis for further research in this area., Competing Interests: Declaration of competing interest The authors declare no competing financial interest., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Understanding what amino acids in α-1,6-glucanases target α-1,6 glycosidic bonds of polysaccharides is timely and important for generating products with branch structure. With this objective, we investigated 330 sequences from seven subfamilies to excavate amino acids for recognition or catalysis of α-1,6 glycosidic bonds. Computational analysis identified two amino acids, E343 and W521, trigger α-1,6 glycosidic bond specificity of enzymes. To explore the effect of E343 and W521 on the product structure, several engineered mutants were studied in our research. Product structural analysis showed that the ratio of amylose and amylopectin is obviously different. The catalytic mechanism revealed that the bulky aromatic side chain is a trigger that controls the ratio of branch glucans. The E148 acts as a proton donor to regulate the generation of branched structures in the product during transglycosidation of the glucan branching enzyme (GBE)., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Ltd. All rights reserved.)

Rice noodle with excellent edible quality usually needs a dense gel network structure, but the dense structure is detrimental to the entry of water molecules during dried rice noodle rehydration. To combine the conflict requirements, we described the branching modification of rice starch using 1,4- α- glucan branching enzyme (GBE). Highly branched starch with a short cluster structure reduced fractal dimension and crystallite thickness while increasing mesh size and hydrophilicity of rice noodle gel network. Rice noodles derived from rice soaked with 128 U/g of GBE had a desirable rehydration time (370 s), which was reduced by 39.84% compared to the control. Meanwhile, the shorter double helix formed by the short cluster contributed to the improved short-range order, resulting in GBE-modified rice noodles with significantly higher tensile strength than control. These findings demonstrate that manipulating the branching degree of starch is an effective method for producing high-quality instant rice noodles., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

Enzymatically rearranging α-1,4 and α-1,6 glycosidic bonds in starch is a green approach to regulating its digestibility. A two-step modification process successively catalyzed by 1,4-α-glucan branching enzymes (GBEs) from Rhodothermus obamensi STB05 (Ro-GBE) and Geobacillus thermoglucosidans STB02 (Gt-GBE) was investigated as a strategy to reduce the digestibility of corn starch. This dual GBE modification process caused a reduction of 25.8 % in rapidly digestible starch fraction in corn starch, which were more effective than single GBE-catalyzed modification with the same duration. Structural analysis indicated that the dual GBE modified product contained higher branching density, more abundant short branches, and shorter external chains than those in single GBE-modified product. These results demonstrated that a moderate Ro-GBE treatment prior to starch gelatinization caused several suitable alterations in starch molecules, which promoted the transglycosylation efficiency of the following Gt-GBE treatment. This dual GBE-catalyzed modification process offered an efficient strategy for regulating starch digestibility., (Copyright © 2021 Elsevier Ltd. All rights reserved.)