Hongjuan Li

Identification of Antifungal Compounds Produced by Lactobacillus casei AST18

Lactobacillus casei AST18 was screened as an antifungal lactic acid bacteria which we have reported before. In this research, the antifungal properties of cell-free culture filtrate (CCF) from L. casei AST18 were detected, and the antifungal compounds of CCF were prepared by ultrafiltration, and semi-preparative HPLC, and then determined by GC–MS. CCF was sensitive to pH and heat treatment but it was not affected by the treatment of trypsin and pepsin. Through the treatment of ultrafiltration and semi-preparative HPLC there were two parts of CCF which showed antifungal activities: part 1 and part 4. Lactic acid was identified as the main antifungal compound in part 1. In part 4, three small molecular substances were detected with GC–MS. The three potential antifungal substances were cyclo-(Leu-Pro), 2,6-diphenyl-piperidine, and 5,10-diethoxy-2,3,7,8-tetrahydro-1H,6H-dipyrrolo[1,2-a;1′,2′-d]pyrazine. The antifungal activity of L. casei AST18 was a synergistic effect of lactic acid and cyclopeptides.

Effect of power ultrasound pretreatment on peptidic profiles and angiotensin converting enzyme inhibition of milk protein concentrate hydrolysates

BACKGROUND The use of power ultrasound as a pretreatment to enhance the hydrolysis of milk protein concentrate (MPC) and subsequent angiotensin converting enzyme (ACE) inhibitory activity has been studied. Liquid chromatography was used to analyse peptide profiles of Neutrase-derived MPC hydrolysates after pretreatment at 0, 1, 3, 5 and 8 min at an ultrasound power level of 800 W. RESULTS The peptide profiles indicated an increase in number of peptides when ultrasound pretreatment was applied. There was also an increase in the degree of hydrolysis of MPC hydrolysates. The profiles indicated that new small peptides in ultrasound pretreated samples (1-5 min) which were not present in the control samples and 8 min pretreated samples, could be responsible for increased ACE inhibitory activity. These small peptides were digested in the 8 min pretreated samples. CONCLUSION Ultrasound pretreatment of MPC increases the ACE inhibitory activity of the hydrolysates because of the production of new small peptides. This can be used as a means to derive potent ACE inhibitory peptides at industrial scale in complex protein sources.

Functionality of milk protein concentrate 80 with emulsifying salts and its applications in analogue cheeses

ABSTRACT Milk protein concentrate 80 (MPC80) was prepared with different emulsifying salts (ES). The effects on particle size (D50), solubility, and surface hydrophobicity (H0) of MPC80 were then observed after production. The molecular weight and secondary structure of MPC80 protein were also investigated through sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier Transform Infrared (FTIR) spectrometry. Particle size (D50) was reduced from 31.37 to 20.67 μm following the addition of sodium phosphate (SPS). The solubility of MPC80 fortified with sodium citrate salt (SCS), SPS, and sodium pyrophosphate (SPP) was improved by 80.32, 78.23, and 55.80%, respectively. The SDS-PAGE pattern showed no significant difference between the control and single-ES-fortified samples, but major protein bands (αs-CN, β-CN, κ-CN, BSA, and β-LG) had a stronger intensity than binary-ES-fortified MPC80. The FTIR results showed that the β-sheet content of ES-fortified MPC80 was relatively higher than that in the control. Compared with analogue cheeses made by MPC80 with and without ES, SCS–SPP (92:8)-modified MPC80 presented a better fluid mass and homogeneous colour.