Characterization of the Aroma-Active Compounds in Commercial Fragrant Rapeseed Oils via Monolithic Material Sorptive Extraction.

Commercial fragrant rapeseed oil (CFRO), from roasted and hot-pressed seeds, is enjoyed in China for its unique aroma. However, the characteristic of aroma-active compounds in CFRO is still unclear. In this study, a new odor monolithic material sorptive extraction method was established to trap volatiles from rapeseed oil. Thirty CFROs were investigated using this method coupled with gas chromatography-mass spectrometry. A total of 29 volatile compounds were identified by gas chromatography-olfactometry including pyrazines, alcohols, aldehydes, ketones, and sulfur compounds. Further, 2,5-dimethylpyrazine (peanut-like), 3-ethyl-2,5-dimethylpyrazine (roasted nut-like), dimethyl trisulfide (cabbage-like), 4-isothiocyanato-1-butene (pungent and pickle-like), butyrolactone (caramel-like), and benzyl nitrile (pungent and sulfur-like) are affirmed as the key odorants for the overall aroma of CFRO, owing to their odor activity values ≥1. This work provides a new insight on acquiring aroma-active compounds from rapeseed oil in a more time-effective process compared to conventional methods. Futhermore, this novel approach is applicable in the field of food flavor.

Novel amphiphilic polyvinylpyrrolidone functionalized silicone particles as carrier for low-cost lipase immobilization.

The high catalytic activity, specificity and stability of immobilized lipase have been attracting great interest. How to reduce the cost of support materials has always been a hot topic in this field. Herein, for the development of low-cost immobilized lipase, we demonstrate an amphiphilic polyvinylpyrrolidone (PVP) grafted on silicone particle (SP) surface materials (SP-PVP) with a rational design based on interfacial activation and solution polymerization. Meanwhile, hydrophilic pristine SP and hydrophobic polystyrene-corded silicone particles (SP-Pst) were also prepared for lipase immobilization. SP-PVP was characterized by X-ray diffraction, scanning electron microscopy, X-ray photoelectron spectroscopy, Fourier transform infrared spectroscopy and thermogravimetry. Our results indicated that the lipase loading amount on the SP-PVP composites was about 215 mg of protein per gram. In the activity assay, the immobilized lipase SP-PVP@CRL exhibited higher catalysis activity and better thermostability and reusability than SP@CRL and SP-Pst@CRL. The immobilized lipase retained more than 54% of its initial activity after 10 times of re-use and approximately trended to a steady rate in the following cycles. By introducing the interesting amphiphilic polymer to this cheap and easily obtained SP surface, the relative performance of the immobilized lipase can be significantly improved, facilitating interactions between the low-cost support materials and lipase.