Vibration mill-assisted complex enzyme hydrolysis for flavoring of freeze-dried sea cucumber powder.

This study aims to analyze the flavor differences of freeze-dried sea cucumber powder, processed for different time intervals, under vibration mill-assisted complex enzyme hydrolysis using electronic nose (E-nose) and gas chromatography-ion mobility spectrometry (GC-IMS). The results of principal component analysis by E-nose showed distinction among the four groups of freeze-dried sea cucumber powder (papain-neutral protease (PN) and flavorzyme-neutral protease (FN), processed for 60 and 80 min). The GC-IMS revealed 35 volatile compounds. Subsequently, based on the fingerprint and heat map results, the flavor differences among the samples were clearly distinguished. When compared to the other three groups, the 60-FN group exhibited a greater variety and quantity of volatile compounds such as octanal, heptanal, hexanal, (E, Z)-2,6-nonadienal, and nonanal. The 80-PN group exhibited high amounts of 2-propanone, ethylbenzene, ethyl acetate, and 2,5-dimethylpyrazine. In addition, the vibration mill technique was considered to be a mild enzyme-assisted method. PRACTICAL APPLICATIONS: This study found that different enzyme types and physical technology operation time can affect the different volatile flavor compounds of freeze-dried sea cucumber powder, which can be quickly and effectively be identified by E-nose and GC-IMS technology to improve the flavor and quality of the product, while facilitating the rapid adjustment and development of the industry. Meanwhile, the results of the study could provide a reference for the deep processing and flavor improvement of the sea cucumber industry and make an important contribution to the related literature. In addition, this could also promote the development and application of non-thermal processing technologies such as vibratory mill in the freeze-dried sea cucumber powder industry.

Changes in the digestion properties and protein conformation of sturgeon myofibrillar protein treated by low temperature vacuum heating during in vitro digestion.

The digestion properties of sturgeon myofibrillar protein (MF) treated by low temperature vacuum heating (LTVH) at different processing temperatures (50, 60 and 70 °C) and times (15 and 30 min) were studied and compared with those of sturgeon MF treated by traditional cooking (TC). The results showed that as the temperature and time increased, the protein digestibility decreased, whereas the particle size and protein aggregation increased. It was observed that the band intensity of myosin heavy chain and myosin heavy chain 7 weakened; however, the band intensity of actin showed little change. MALDI-TOF-MS analysis revealed that the digested products of the samples treated by LTVH had a larger proportion of 750-1000 Da peptides than those treated by TC, which was consistent with the trend of the number of unique peptides identified in each group. Fourier transmission infrared (FT-IR) spectroscopy showed that the contents of α-helices and ß-sheets exhibited negative and positive correlations with the temperature, respectively. Overall, compared to TC, LTVH can relieve the heat stress of protein conformation, reduce protein aggregation to improve the accessibility of the protein to digestive protease, and increase digestibility.