Structural and functional variations of octenyl succinylated clustered amylopectin produced by distinctive glycogen branching enzymes

• Published in: Food science and biotechnology Vol. 34; no. 11; pp. 2445 - 2453
• Main Authors: Choi, Kyeong-Ok, Yim, Cheul-Soon, Nguyen, Phu Cuong, Park, Jong-Tae
• Format: Journal Article
• Language: English
• Published: Korea (South) Springer Nature B.V 01.07.2025; 한국식품과학회
• Subjects: Amylopectin; Degree of polymerization; E coli; Enzymes; Esterification; Glycogen; Glycogens; Infrared spectroscopy; Molecular weight; NMR; Nuclear magnetic resonance; Structure-function relationships; 식품과학; Octenyl succinic anhydride; Clustered amylopectin; Functional enhancement; Glycogen branching enzyme; OSA-modified starch
• ISSN: 1226-7708; 2092-6456; 2092-6456
• DOI: 10.1007/s10068-025-01892-1

Clustered amylopectins (CAPs) were produced using recombinant glycogen branching enzymes from K12 (EcGBE) and (VvGBE). The CAPs were esterified with octenyl succinic anhydride (OSA), introducing novel functional characteristics. Vv-CAP demonstrated a reduced apparent molecular weight and a higher prevalence of both short (degree of polymerization (DP) ≤ 5, 13.3%) and medium branches (5 < DP ≤ 12, 58.2%) compared to Ec-CAP. FT-IR spectra confirmed the successful esterification of CAPs with OSA. H-NMR analysis showed the degree of substitution (DS) for OSA-CAPs varied based on the CAP to OSA ratio (DS 0.021-0.058 for Ec-CAP and 0.011-0.066 for Vv-CAP). Esterification with OSA on shortened branches resulted in a slower digestion rate and increased resistant starch proportion. Additionally, this process enhanced the emulsifying properties of CAPs and improved the aqueous solubility of puerarin. OSA-modified CAPs are promising for pharmaceutical applications. The online version contains supplementary material available at 10.1007/s10068-025-01892-1.