Enhancing vitamin D3 bioaccessibility: Unveiling hydrophobic interactions in soybean protein isolate and vitamin D3 binding via an infant in vitro digestion model.

In the domain of infant nutrition, optimizing the absorption of crucial nutrients such as vitamin D3 (VD3) is paramount. This study harnessed dynamic-high-pressure microfluidization (DHPM) on soybean protein isolate (SPI) to engineer SPI-VD3 nanoparticles for fortifying yogurt. Characterized by notable binding affinity (Ka = 0.166 × 105 L·mol-1) at 80 MPa and significant surface hydrophobicity (H0 = 3494), these nanoparticles demonstrated promising attributes through molecular simulations. During simulated infant digestion, the 80 MPa DHPM-treated nanoparticles showcased an impressive 74.4% VD3 bioaccessibility, delineating the pivotal roles of hydrophobicity, bioaccessibility, and micellization dynamics. Noteworthy was their traversal through the gastrointestinal tract, illuminating bile salts' crucial function in facilitating VD3 re-encapsulation, thereby mitigating crystallization and augmenting absorption. Moreover, DHPM treatment imparted enhancements in nanoparticle integrity and hydrophobic properties, consequently amplifying VD3 bioavailability. This investigation underscores the potential of SPI-VD3 nanoparticles in bolstering VD3 absorption, thereby furnishing invaluable insights for tailored infant nutrition formulations.

Glycation-induced enhancement of yeast cell protein for improved stability and curcumin delivery in Pickering high internal phase emulsions.

Pickering high internal phase emulsions (HIPEs) have gained significant attention for various applications within the food industry. Yeast cell protein (YCP), derived from spent brewer's yeast, stands out as a preferred stabilizing agent due to its cost-effectiveness, abundance, and safety profile. However, challenges persist in utilizing YCP, notably its instability under high salt concentration, thermal processing, and proximity to its isoelectric point. This study aimed to enhance YCP's emulsifying properties through glycation with glucose and evaluate its efficacy as a stabilizer for curcumin (CUR)-loaded HIPEs. The results revealed that glycation increased YCP's surface hydrophobicity, exposing hydrophobic groups. This augmentation, along with steric hindrance from grafted glucose molecules, improved emulsifying properties, resulting in a thicker interfacial layer around oil droplets. This fortified interfacial layer, in synergy with steric hindrance, bolstered resistance to pH changes, salt ions, and thermal degradation. Moreover, HIPEs stabilized with glycated YCP exhibited reduced oxidation rates and improved CUR protection. In vitro digestion studies demonstrated enhanced CUR bioaccessibility, attributed to a faster release of fatty acids. This study underscores the efficacy of glycation as a strategic approach to augment the applicability of biomass proteins, exemplified by glycated YCP, in formulating stable and functional HIPEs for diverse food applications.

Purification and Characterization of the Enzyme Fucoidanase from Cobetia amphilecti Utilizing Fucoidan from Undaria pinnatifida.

Fucoidanase is an unstable enzyme with high specificity that requires a large about of time to screen it from microorganisms. In this study, enzymatic hydrolysis was used to produce low-molecular-weight fucoidan from microorganisms via the degradation of high-molecular-weight fucoidan without damage to the sulfate esterification structure of oligosaccharide. The microbial strain HN-25 was isolated from sea mud and was made to undergo mutagenicity under ultraviolet light. Fucoidanase was extracted via ultrasonication and its enzymatic activity was improved via optimization of the ultrasonic conditions. The enzymatic properties and degradation efficiency of fucoidanase were characterized. The microbial strain HN-25 is a Gram-negative aerobic and rod-shaped-cell bacterium, and therefore was identified as Cobetia amphilecti via 16s rDNA. The results proved that fucoidanase is a hydrolytic enzyme with a molecular weight of 35 kDa and with high activity and stability at 30 °C and pH 8.0. The activity of fucoidanase was significantly enhanced by sodium and calcium ions and inhibited by a copper ion and ethylenediaminetetraacetate (EDTA). There was a significant decrease in the molecular weight of fucoidan after enzymatic hydrolysis. The low-molecular-weight fuicodan was divided into four fractions, mainly concentrated at F3 (20~10 kDa) and F4 (≤6 kDa). These consequences suggest that fucoidanase obtained from Cobetia amphilecti is stable and efficient and could be a good tool in the production of bioactive compounds.

Development of an indirect ELISA to detect PEDV specific IgA antibody based on a PEDV epidemic strain.

BACKGROUND: Porcine epidemic diarrhea (PED), a swine epidemic disease caused by porcine epidemic diarrhea virus (PEDV), is characterized by severe watery diarrhea, vomiting, dehydration and high mortality in piglets, and has caused serious economic losses to the global porcine industry. The level of PEDV IgA antibody is a key marker to assess the extent of passive immunity of the resistance against PEDV infection. However, current commercial structure proteins-based kits for detection of PEDV antibody are not affordable, and those kits require complicated antigen preparation procedures, which cannot meet the scope of economic benefits of many large-scale pig companies in China. Therefore, there is an urgent need to develop an accurate, simple, and economical method for IgA detection in clinical samples. In this study, an indirect ELISA (i-ELISA) method was developed based on a purified PEDV epidemic strain (NH-TA2020). RESULTS: The results show that optimal working dilution ratios of PEDV antigen and HRP anti-swine IgA are at 1: 1000 and 1:15000 respectively. The sensitivity of this method is high with the maximum dilution of samples up to 1:160, and coefficients of variation (CV) of both the intra assays and inter assays were no more than 15%. In addition, the relative sensitivities of the i-ELISA were above 90% compared with values from commercial kits in both serum and oral fluid samples. CONCLUSIONS: Our results suggested that the i-ELISA developed in this study was an accurate, simple, and economical method for PEDV-IgA detection in clinical samples.

Efficient encapsulation of curcumin into spent brewer's yeast using a pH-driven method.

Curcumin (CUR) was encapsulated into yeast cells (YCs) through a pH-driven method with a 5.04-fold increase in loading capacity and a 43.63-fold reduction in incubation time compared to the conventional diffusion method. Optimal encapsulation was obtained when the mass ratio of CUR to YCs was 0.1, and the loading capacity and encapsulation efficiency were 8.07% and 80.66%, respectively. Encapsulation of CUR into YCs was confirmed by fluorescence microscopy, differential scanning calorimetry, and thermogravimetric analysis. Fourier transform infrared spectroscopy and X-ray diffraction further demonstrated that the encapsulated CUR was interacted with mannoprotein and ß-glucan of the cell wall network through hydrophobic interaction and hydrogen bond in amorphous state. The in vitro bioaccessibility of YCs-loaded CUR was significantly increased by 6.05-fold. The enhanced encapsulation efficiency and rapid encapsulation process proposed in this study could facilitate YCs-based microcarriers to encapsulate bioactive substances with higher bioaccessibility.

A combination of HA and PA mutations enhances virulence in a mouse-adapted H6N6 influenza A virus.

UNLABELLED: H6N6 viruses are commonly isolated from domestic ducks, and avian-to-swine transmissions of H6N6 viruses have been detected in China. Whether subsequent adaptation of H6N6 viruses in mammals would increase their pathogenicity toward humans is not known. To address this, we generated a mouse-adapted (MA) swine influenza H6N6 virus (A/swine/Guangdong/K6/2010 [GDK6-MA]) which exhibited greater virulence than the wild-type virus (GDK6). Amino acid substitutions in PB2 (E627K), PA (I38M), and hemagglutinin ([HA] L111F, H156N, and S263R) occurred in GDK6-MA. HA with the H156N mutation [HA(H156N)] resulted in enlarged plaque sizes on MDCK cells and enhanced early-stage viral replication in mammalian cells. PA(I38M) raised polymerase activity in vitro but did not change virus replication in either mammalian cells or mice. These single substitutions had only limited effects on virulence; however, a combination of HA(H156N S263R) with PA(I38M) in the GDK6 backbone led to a significantly more virulent variant. This suggests that these substitutions can compensate for the lack of PB2(627K) and modulate virulence, revealing a new determinant of pathogenicity for H6N6 viruses in mice, which might also pose a threat to human health. IMPORTANCE: Avian H6N6 influenza viruses are enzootic in domestic ducks and have been detected in swine in China. Infections of mammals by H6N6 viruses raise the possibility of viral adaptation and increasing pathogenicity in the new hosts. To examine the molecular mechanisms of adaptation, a mouse-adapted avian-origin swine influenza H6N6 virus (GDK6-MA), which had higher virulence than its parental virus, was generated. Specific mutations were found in PB2 (E627K), PA (I38M), and HA (L111F, H156N, and S263R) and were assessed for their virulence in mice. The combination of HA(H156N S263R) and PA(I38M) compensated for the lack of PB2(627K) and showed increased pathogenicity in mice, revealing a novel mechanism that can affect the virulence of influenza viruses. H6N6 viruses should be monitored in the field for more virulent forms that could threaten human health.

Genetic characterization of avian-origin H3N2 canine influenza viruses isolated from Guangdong during 2006-2012.

Canine influenza virus (CIV) is an emerging pathogen that causes severe and acute respiratory disease in dogs. In 2006, the H3N2 canine influenza virus was first identified in dogs from Guangdong province in China. Up to now, nine CIVs have been isolated from different populations in Guangdong. The nine isolates were grouped together with the canine H3N2 viruses isolated from dogs and felines in Korea, when the eight phylogenetic trees constructed were compared. These findings emphasize the importance of CIV surveillance in this region for understanding the genesis of this virus, and it is important to remain aware of the potential of H3N2 CIV to be transmitted from dogs to the human population.

Lack of evidence of avian-to-human transmission of avian influenza A (H5N1) virus among veterinarians, Guangdong, China, 2012.

BACKGROUND: Cases of human infections with H5N1 avian influenza viruses have been reported all over the world with the reason of direct contact with sick or diseased poultry, which suggests the direct contact with poultry may be one of the major risk factors for human infection. OBJECTIVES: In this study, we estimated the seroprevalence of antibodies against avian influenza A (H5N1) virus in veterinarians with exposure to avians. STUDY DESIGN: From May 21, 2011 through April 22, 2012, 406 veterinarians exposure to poultry in Guangdong province were interviewed a questionnaire. A serum specimen was collected from participants to test for H5N1 antibodies by HI and NT assay. RESULTS: None of the 406 sera from occupationally exposed veterinarians was positive according to the HI test and the NT test with the H5N1 AIV. CONCLUSION: Our seroepidemiologic survey suggests that the risk of avian-to-human transmission of the H5N1 AIV is very low based on the samples that we tested. However, prevention regarding the risk of H5N1 AIV transmission is essential and should be recommended as public health measures.