Changes in the structural and physicochemical characterization of pea starch modified by Bacillus-produced α-amylase

In this study, changes in structural and physicochemical properties of pea starch treated with Bacillus-produced α-amylase were determined. The results showed that enzymatically modified pea starch had lower amylose content and granule size but higher branching degree and relative crystallinity. After enzyme hydrolysis, the distribution of A and B1 chains slightly decreased, while the distribution of B2 and B3 chains increased lightly. Enzymatic hydrolysis preferentially occurred in the amorphous region and cannot change the crystalline structure of pea starch. Moreover, pea starch showed lower light transmittance, peak viscosity, breakdown viscosity, pasting temperature, shear viscosity, storage modulus and loss modulus, while the oil adsorption capacity and gelatinization enthalpy significantly increased with increasing α-amylase hydrolysis time. Correlation analysis indicated that α-amylase hydrolysis had different effects on different pea varieties. This research could provide ideas for exploring new applications for enzymatically modified pea starch in food industry.Industrial relevanceThis study found that Bacillus-produced α-amylase significantly changed the amylose content, granule size and viscosity of pea starch, which was helpful to further investigate the modified starch. This technology is expected to widen the applications of pea starch modified by Bacillus-produced α-amylase in food industry, for example as thickener, stabilizer and beverage, to improve the texture, stability and shelf-life of various food products.     

Reaction kinetics study of α-amylase in the hydrolysis of starch size on cotton fabrics

A study of tension surging and of the properties of the resultant yarns is reported. Tension profiles are discussed and assigned to three modes of operation, namely, pre-surging, surging, and post-surging. The critical conditions for these three modes and the wavelengths and amplitude of tension surging are investigated. The insertion of twist is examined, and it is shown that, not only is the surging mode unstable, hut there is also a higher-frequency instability in the post-surging mode. On the basis of the results obtained from routine tests for textured yarns, it is confirmed that the quality of the yarns resulting from both surging and post-surging modes is not acceptable.     

Identification of an acidic α-amylase from Alicyclobacillus sp. A4 and assessment of its application in the starch industry

An acidic α-amylase was purified from thermoacidophilic Alicyclobacillus sp. A4 by ion exchange chromatography with 22% recovery, and showed a molecular mass of 64 kDa by SDS-PAGE. Its amino acid sequence was determined by sequencing three internal peptides and the complete genome of strain A4, and shared highest identity (64%) with Alicyclobacillusacidocaldarius α-amylase. Compared with other reported α-amylases, the purified enzyme had some distinct characteristics. The optimal activity was found to occur at 75 °C and pH 4.2, similar to the glucamylase widely used in the starch industry. The enzyme was Ca²⁺ independent, and had strong ability to digest raw starch (96.71%) with commercial glucamylase in one step. These properties of the purified enzyme make up the deficiency of the commercial α-amylases currently used and avoid repeated adjustment of pH and temperature in double-enzymatic sugar-making process. The purified enzyme will be commercially valuable in the starch industry.     

Physicochemical properties, α-amylase and α-glucosidase inhibitory effects of the polysaccharide from leaves of Morus alba L. under simulated gastro-intestinal digestion and its fermentation capability in vitro by human gut microbiota

The investigation aimed at determining the impact of sequential simulated digestion on the physicochemical properties and digestive enzymes inhibitory effects of the polysaccharides fraction (MLP-2) of Morus alba L. leaves as well as its in vitro fermentation behaviours. After artificial salivary, gastric and intestinal digestions, the chemical components and microstructure of MLP-2 were altered with significantly (P < 0.05) decreased molecular weight. The α-amylase and α-glucosidase inhibitory activities of MLP-2 were significantly (P < 0.05) improved throughout simulated digestion. MLP-2I, the intestinal digested fraction of MLP-2, could significantly (P < 0.05) decrease the pH value of fermented culture and increase the short-chain fatty acids (SCFA) concentrations, especially acetic, propionic and butyric acids. In conclusion, MLP-2 could be gradually degraded under simulated digestion with altered physicochemical properties and enhanced α-amylase and α-glucosidase inhibitory effects, and further utilised by human gut microbiota to decrease pH value and promote SCFA production.