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Valorizing protein-polysaccharide conjugates from sugar beet pulp as an emulsifier.
Lin, Jiawei; Tang, Zhong-Sheng; Brennan, Charles Stephen; Chandrapala, Jayani; Gao, Wenhong; Han, Zhong; Zeng, Xin-An.
Affiliation
  • Lin J; School of Food Sciences and Engineering, South China University of Technology, Guangzhou 510640, China.
  • Tang ZS; College of Food Science and Engineering, Guangdong Ocean University, Yangjiang 529500, China.
  • Brennan CS; School of Science, RMIT University, GPO Box 2474, Melbourne, VIC 3001, Australia.
  • Chandrapala J; School of Science, RMIT University, GPO Box 2474, Melbourne, VIC 3001, Australia.
  • Gao W; School of Food Sciences and Engineering, South China University of Technology, Guangzhou 510640, China.
  • Han Z; School of Food Sciences and Engineering, South China University of Technology, Guangzhou 510640, China; Guangdong Provincial Key Laboratory of Intelligent Food Manufacturing, Foshan University, Foshan 528225, China.
  • Zeng XA; School of Food Sciences and Engineering, South China University of Technology, Guangzhou 510640, China; Guangdong Provincial Key Laboratory of Intelligent Food Manufacturing, Foshan University, Foshan 528225, China; Yangjiang Research Institute, South China University of Technology, Yangjiang 529500
Int J Biol Macromol ; 226: 679-689, 2023 Jan 31.
Article in En | MEDLINE | ID: mdl-36436597
ABSTRACT
Inspired by the emulsion stability of sugar beet pulp pectin, the hydrophobic protein fraction in sugar beet pulp (SBP) is expected to feature high interfacial activity. This work retrieved alkaline extracted protein-polysaccharide conjugates (AEC) from partially depectinized SBP by hot alkaline extraction. AEC was protein-rich (57.20 %), and the polysaccharide mainly comprised neutral sugar, which adopted a rhamnogalacturonan-I pectin-like structure. The hydrophobic polypeptide chains tangled as a dense 'core' with polysaccharide chains attached as a hydrated 'shell' (hydrodynamic radius of ~110 nm). AEC could significantly decrease the oil-water interfacial tension (11.58 mN/m), featuring superior emulsification performance than three control emulsifiers, especially the excellent emulsifying stability (10 % oil) as the emulsion droplet size of 0.438 and 0.479 µm for fresh and stored (60 °C, 5 d) emulsions, respectively. The relationship of molecular structure to emulsification was investigated by specific enzymic modification, suggesting the intact macromolecular structure was closely related to emulsifying activity and that the NS fraction contributed greatly to emulsifying stability. Moreover, AEC was highly efficient to stabilize gel-like high internal phase emulsions (oil fraction 0.80) with low concentration (0.2 %) and even high ionic strength (0-1000 mM). Altogether, valorizing AEC as an emulsifier is feasible for high-value utilization of SBP.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Beta vulgaris Language: En Journal: Int J Biol Macromol Year: 2023 Document type: Article Affiliation country: China

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Beta vulgaris Language: En Journal: Int J Biol Macromol Year: 2023 Document type: Article Affiliation country: China