Aspergillus oryzae β-D-galactosidase immobilization on glutaraldehyde pre-activated amino-functionalized magnetic mesoporous silica: Performance, characteristics, and application in the preparation of sesaminol.

Aspergillus oryzae β-D-galactosidase (β-Gal) efficiently hydrolyzes sesaminol triglucoside into sesaminol, which has higher biological activity. However, β-Gal is difficult to be separate from the reaction mixture and limited by stability. To resolve these problems, β-Gal was immobilized on amino-functionalized magnetic nanoparticles mesoporous silica pre-activated with glutaraldehyde (FeO@mSiO-β-Gal), which was used for the first time to prepare sesaminol.

Effects of Steam and Water Blanching on Drying Characteristics, Water Distribution, Microstructure, and Bioactive Components of .

In the current work, the effects of steam and boiling water blanching on the drying characteristics, water distribution, microstructure, and contents of bioactive substances of () were explored. Results showed that the degree of steaming and blanching was related to the core temperature of . The steaming and blanching pretreatment increased the drying time of the samples by more than 50%.

Characterization of Peanut Protein Hydrolysate and Structural Identification of Umami-Enhancing Peptides.

Umami peptides are naturally found in various foods and have been proven to be essential components contributing to food taste. Defatted peanut powder hydrolysate produced by a multiprotease (Flavorzyme, Alcalase, and Protamex) was found to elicit an umami taste and umami-enhancing effect. The taste profiles, hydrolysis efficiency, amino acids, molecular weight distribution, Fourier transform infrared spectroscopy (FT-IR), and separation fractions obtained by ultrafiltration were evaluated.

Flavonoid constituents of Crevost et Lemarie and their antioxidant and antidiabetic effects in diabetic rats - and studies.

Crevost et Lemarie () is a well-known dietary spice and traditional Chinese medicine. This study aimed to identify the flavonoids in and evaluate their antioxidant and antidiabetic activities in and studies. methanol extracts possessed a high flavonoid content (1.

Dual-enzyme hydrolysis for preparation of ACE-inhibitory peptides from sesame seed protein: Optimization, separation, and identification.

To prepare and identify ACE-inhibitory peptides originated from sesame seed protein, peptides with strong ACE-inhibitory activities were obtained via the optimization of protease and hydrolysis conditions, and these peptides were purified and identified by membrane separation, gel filtration, and liquid chromatography-mass spectrometry. Results showed that the dual-enzyme comprised alcalase and trypsin with the enzyme activity ratio of 3:7 was suitable to produce ACE-inhibitory peptides. The highest ACE-inhibitory activity of 98.

Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame ( L.) Protein and Molecular Docking Study.

The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and α-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time.

Extraction, identification and structure-activity relationship of antioxidant peptides from sesame (Sesamum indicum L.) protein hydrolysate.

To elucidate the sequence, origin and structure-activity relationship of antioxidant peptides from sesame protein, sesame protein was hydrolysed by a dual-enzyme system comprised alcalase and trypsin, then this hydrolysate was fractionated by ultrafiltration and preparative HPLC. Subsequently, peptides in the high antioxidant activity fraction were identified by nano liquid chromatography-electrospray ionization-tandem mass spectrometry (Nano-LC-ESI-MS/MS), finally the structure-activity relationship of antioxidant peptide with the strongest activity in the sesame peptides was illustrated by comparative molecular field analysis (CoMFA). The results showed that seven novel antioxidant peptides were discovered, their sequences were as follows, RDRHQKIG, TDRHQKLR, MNDRVNQGE, RENIDKPSRA, SYPTECRMR, GGVPRSGEQEQQ and AGEQGFEYVTFR.