Improving the microbiological safety and quality of aquatic products using nonthermal processing.

Spoilage and deterioration of aquatic products during storage are inevitable, posing significant challenges to their suitability for consumption and the sustainability of the aquatic products supply chain. Research on the nonthermal processing of fruit juices, probiotics, dairy products, and meat has demonstrated positive outcomes in preserving quality. This review examines specific spoilage bacteria species and mechanisms for various aquatic products and discusses the principles, characteristics, and applications of six nonthermal processing methods for bacterial inhibition to maintain microbiological safety and physicochemical quality. The primary spoilage bacteria groups differ among fish, crustaceans, and shellfish based on storage conditions and durations. Four metabolic pathways utilized by spoilage microorganisms-peptides and amino acids, nitrogen compounds, nucleotides, and carbohydrates-are crucial in explaining spoilage. Nonthermal processing techniques, such as ultrahigh pressure, irradiation, magnetic/electric fields, plasma, and ultrasound, can inactivate microorganisms, thereby enhancing microbiological safety, physicochemical quality, and shelf life. Future research may integrate nonthermal processing with other technologies (e.g., modified atmosphere packaging and omics) to elucidate mechanisms of spoilage and improve the storage quality of aquatic products.

Current progress of emerging technologies in human and animals' milk processing: Retention of immune-active components and microbial safety.

Human milk and commercial dairy products play a vital role in humans, as they can provide almost all essential nutrients and immune-active components for the development of children. However, how to retain more native immune-active components of milk during processing remains a big question for the dairy industry. Nonthermal technologies for milk processing are gaining increasing interest in both academic and industrial fields, as it is known that thermal processing may negatively affect the quality of milk products. Thermosensitive components, such as lactoferrin, immunoglobulins (Igs), growth factors, and hormones, are highly important for the healthy development of newborns. In addition to product quality, thermal processing also causes environmental problems, such as high energy consumption and greenhouse gas (GHG) emissions. This review summarizes the recent advances of UV-C, ultrasonication (US), high-pressure processing (HPP), and other emerging technologies for milk processing from the perspective of immune-active components retention and microbial safety, focusing on human, bovine, goat, camel, sheep, and donkey milk. Also, the detailed application, including the instrumental design, technical parameters, and obtained results, are discussed. Finally, future prospects and current limitations of nonthermal techniques as applied in milk processing are discussed. This review thereby describes the current state-of-the-art in nonthermal milk processing techniques and will inspire the development of such techniques for in-practice applications in milk processing.

Proteomic Comparisons of Caprine Milk Whole Cream Buttermilk Whey and Cheese Whey Cream Buttermilk.

Buttermilk, a potential material used to produce milk fat globule membrane (MFGM), is obtained as a byproduct of butter making from milk whole cream and cheese whey cream. This study investigated the effects of rennet and acid coagulation on the protein profiles of buttermilk rennet-coagulated whey (BRW) and buttermilk acid-coagulated whey (BAW). They were compared to those of whey cream buttermilk (WCB). Rennet coagulation was more efficient in removing casein, while retaining more IgG and lactoferrin than acid coagulation. BRW had more MFGM than BAW. Butyrophilin, xanthine dehydrogenase, and mucin1 were significantly higher (P < 0.05) in BRW, while fatty acid-binding protein 3 was enriched in BAW. KEGG analysis showed that complement and coagulation cascades had the greatest differences, and the abundance of proteins involved in this signaling pathway in BRW and BAW was higher, suggesting their potential anticoagulant and anti-inflammatory activity. BAW had higher apolipoprotein A4 and transcobalamin 2, which are essential carriers for transporting long-chain fatty acids and vitamin B12 from the intestine to the blood. Therefore, BAW intake might improve lipids and vitamin B12 absorption. This study can help deepen the understanding of protein composition of MFGM-enriched whey and facilitate the production of MFGM proteins for infants and old-aged populations.

Lipidomic Comparisons of Whole Cream Buttermilk Whey and Cheese Whey Cream Buttermilk of Caprine Milk.

Buttermilk is a potential material for the production of a milk fat globule membrane (MFGM) and can be mainly classified into two types: whole cream buttermilk and cheese whey cream buttermilk (WCB). Due to the high casein micelle content of whole cream buttermilk, the removal of casein micelles to improve the purity of MFGM materials is always required. This study investigated the effects of rennet and acid coagulation on the lipid profile of buttermilk rennet-coagulated whey (BRW) and buttermilk acid-coagulated whey (BAW) and compared them with WCB. BRW has significantly higher phospholipids (PLs) and ganglioside contents than BAW and WCB. The abundance of arachidonic acid (ARA)- and eicosapentaenoic acid (EPA)-structured PLs was higher in WCB, while docosahexaenoic acid (DHA)-structured PLs were higher in BRW, indicating that BRW and WCB intake might have a greater effect on improving cardiovascular conditions and neurodevelopment. WCB and BRW had a higher abundance of plasmanyl PL and plasmalogen PL, respectively. Phosphatidylcholine (PC) (28:1), LPE (20:5), and PC (26:0) are characteristic lipids among BRW, BAW, and WCB, and they can be used to distinguish MFGM-enriched whey from different sources.

The combined effect of commercial tilapia collagen peptides and antioxidants against UV-induced skin photoaging in mice.

Chronic over-exposure to UV radiation leads to the damage of skin tissue. The aim of this study was to investigate the effects of collagen peptide (CP) and antioxidant (astaxanthin, vitamin C (Vc), and vitamin E (Ve)) combinations on skin photoaging. Forty male UV-induced BALB/c mice were randomized and fed saline or CP and antioxidants for 7 weeks using gavage feeding. The results showed that oral administration of CP, CP combined with Vc and Ve (VCE) or Haematococcus pluvialis extract (HPE) significantly (P < 0.05) reduced a* of mouse skin and increased the content of Hyp and type I collagen to varying degrees, thereby improving skin integrity. Furthermore, the combination of CP, HPE, and VCE showed increased upregulation of antioxidant enzyme expression, reduced serum ROS, and decreased inhibition of metalloproteinase expression compared to the other treatment groups. Thus, this combination showed better effects in inhibiting collagen degradation and maintaining the redox balance. The Nrf2/ARE and TGF-ß/Smad transcription systems are likely involved in these effects. Therefore, the results suggest that a diet containing CP, astaxanthin, and vitamins might be recommended to improve skin health and appearance.

Gastrointestinal digestibility of micellar casein dispersions: Effects of caprine vs bovine origin, and partial colloidal calcium depletion using in vitro digestion models for the adults and elderly.

In vitro coagulation and digestion of caprine and bovine micellar casein concentrate (MCC) with or without partial colloidal calcium depletion (deCa) were studied under simulated adult and elderly conditions. Gastric clots were smaller and looser for caprine than bovine MCC, and were further looser with deCa and under elderly condition for both caprine and bovine MCC. Casein hydrolysis and concomitant formation of large peptides was faster for caprine than bovine MCC, and with deCa and under adult condition for caprine and bovine MCC. Formation of free amino groups and small peptides were faster for caprine MCC, and with deCa and under adult condition. Upon intestinal digestion, proteolysis occurred rapidly, and was faster under adult condition, but showed less differences with increasing digestion between caprine and bovine MCC, and with and without deCa. These results suggested weakened coagulation and greater digestibility for caprine MCC and MCC with deCa under both conditions.

Temperature-dependent dissociation of human micellar ß-casein: Implications of its phosphorylation degrees and casein micelle structures.

Temperature-dependent dissociation of human micellar ß-casein regarding its phosphorylation degrees and micelle structures were studied. Human milk was fractionated at 25 °C into soluble (S-25 °C) and micellar (M-25 °C) fractions, and the latter was fractionated at 4 °C into soluble (S-4 °C) and micellar (M-4 °C) fractions. ß-casein ratios among S-25 °C, S-4 °C and M-4 °C were 19%, 59% and 22%. ß-casein isoforms were predominated by 0-P, 1-P and 2-P in S-25 °C, by 0-P, 1-P, 2-P and 4-P in S-4 °C, and by 0-P in M-4 °C. For micelles remained after dissociation of ß-casein and calcium, the size increased, molar mass decreased, morphologies were maintained, and internal protein inhomogeneities disappeared, compared with micelles in M-25 °C. ß-casein isoforms with lower phosphorylation degrees may form a frame mainly through hydrophobic interactions, attached with more highly phosphorylated isoforms and colloidal calcium phosphate via calcium bridges for forming human micelle.

Transmission of Major and Minor Serum Proteins during Microfiltration of Skim Milk: Effects of Pore Diameters, Concentration Factors and Processing Stages.

Effects of pore diameters (100, 50, and 20 nm), concentration factors (1-8) and processing stages (1-5) on the transmission of major serum proteins (ß-lactoglobulin and α-lactalbumin) and minor serum proteins (immunoglobulin (Ig) G, IgA, IgM, lactoferrin (LF), lactoperoxidase (LPO), xanthine oxidase (XO)) during ceramic microfiltration (MF) of skim milk were studied. Holstein skim milk was microfiltered at a temperature of 50 °C, a transmembrane pressure of 110 kPa and a crossflow velocity of 6.7 m/s, using a tubular single stainless steel module that consisted of three ceramic tubes, each with 19 channels (3.5 mm inner diameter) and a length of 0.5 m. For MF with 100 nm and 50 nm pore diameters, the recovery yield of major serum proteins in permeate was 44.3% and 44.1%, while the recovery yield of minor serum proteins was slightly less by 0%-8% than 50 nm MF. MF with 20 nm pore diameters showed a markedly lower (by 12%-45%) recovery yield for both major and minor serum proteins, corresponding with its lower membrane flux. Flux sharply decreased with an increasing concentration factor (CF) up to four, and thereafter remained almost unchanged. Compared to the decrease (88%) of flux, the transmission of major and minor serum proteins was decreased by 4%-15% from CF = one to CF = eight. With increasing processing stages, the flux gradually increased, and the recovery yield of both major and minor proteins in the permeate gradually decreased and reached a considerably low value at stage five. After four stages of MF with 100 nm pore diameter and a CF of four for each stage, the cumulative recovery yield of major serum proteins, IgG, IgA, IgM, LF, LPO, and XO reached 95.7%, 90.8%, 68.5%, 34.1%, 15.3%, 39.1% and 81.2% respectively.

Solubilisation of micellar casein powders by high-power ultrasound.

High protein milk ingredients, such as micellar casein powder (MCP), exhibit poor solubility upon reconstitution in water, particularly after long-time storage. In this study, ultrasonication (20 kHz, power density of 0.75 W/ml) was used to improve the solubility of aged MCP powders. For all the MCP powders (concentration varying from 0.5 to 5%, and storage of MCP at 50 °C for up to 10 days) it was found that short time ultrasonication (2.5 min) reduced the size of the protein particles from >30 µm to ∼0.1 µm, as measured by light scattering. This resulted in an improvement of solubility (>95%) for all the MCP powders. Cryo-electron microscopy and small x-ray angle scattering showed that the MCP powders dissolved into particles with morphologies and internal structure similar to native casein micelles in bovine milk. SDS-PAGE and RP-HLPC showed that ultrasonication did not affect the molecular weight of the individual casein molecules. Compared to overhead stirring using a 4-blade stirrer, ultrasonication required less than 10 times the drawn electrical energy density to achieve a particle size 10 times smaller.

Effects of skim milk pre-acidification and retentate pH-restoration on spray-drying performance, physico-chemical and functional properties of milk protein concentrates.

This study investigates the effects of pre-acidification (pH 6.7-5.4) of skim milk, followed by pH-restoration of the retentates, on spray-drying performance, physico-chemical properties and functionality of the resulting milk protein concentrate (MPC). Powder recovery decreased with decreasing pH of pre-acidification but improved with pH-restoration. Colloidal calcium was gradually solubilized with decreasing pH of pre-acidification but was slightly recovered by pH-restoration. Dissociation of micellar caseins increased with decreasing pH of pre-acidification of skim milk and was further increased by pH-restoration. Casein micelles maintained their overall structures at pre-acidification pH of 6.7-6.0, and partially disintegrated into loosely entangled aggregates at pH 5.7-5.4; while after pH-restoration, micelles generally maintained their overall structures at pre-acidification pH of 6.0, and completely disintegrated at pH 5.7-5.4. Solubility and emulsifying properties of MPC improved with decreasing pH of pre-acidification and with pH-restoration. Heat stability of MPC declined with decreasing pH of pre-acidification but improved with pH-restoration.

Effects of enzymatic dephosphorylation on infant in vitro gastrointestinal digestibility of milk protein concentrate.

This study investigated the effects of dephosphorylation extent on infant in vitro gastric clotting property and gastrointestinal digestibility of milk protein concentrate. Dephosphorylation was affected by phosphatase type and incubation pH. A series of milk protein concentrate with 0-69% dephosphorylation were obtained by incubation with calf intestinal alkaline phosphatase at pH 6.5 for 0-420 min. Both ß- and αs1-caseins in the modified milk protein concentrate showed multiply dephosphorylated isoforms with different numbers of phosphate groups depending on the extent of dephosphorylation. With increased dephosphorylation of milk protein concentrate, the gastric clotting extent decreased and the gastrointestinal digestibility increased under infant in vitro conditions. These results suggested the potential of developing a dephosphorylated milk protein concentrate, with improved gastric clotting property and gastrointestinal digestibility, to simulate the multiply phosphorylated patterns of human casein and hence to further the humanization of infant formula on a molecular level.

Collagen and gelatin.

Collagen and gelatin have been widely used in the food, pharmaceutical, and cosmetic industries due to their excellent biocompatibility, easy biodegradability, and weak antigenicity. Fish collagen and gelatin are of renewed interest, owing to the safety and religious concerns of their mammalian counterparts. The structure of collagen has been studied using various modern technologies, and interpretation of the raw data should be done with caution. The structure of collagen may vary with sources and seasons, which may affect its applications and optimal extraction conditions. Numerous studies have investigated the bioactivities and biological effects of collagen, gelatin, and their hydrolysis peptides, using both in vitro and in vivo assay models. In addition to their established nutritional value as a protein source, collagen and collagen-derived products may exert various potential biological activities on cells in the extracellular matrix through the corresponding food-derived peptides after ingestion, and this might justify their applications in dietary supplements and pharmaceutical preparations. Moreover, an increasing number of novel applications have been found for collagen and gelatin. Therefore, this review covers the current understanding of the structure, bioactivities, and biological effects of collagen, gelatin, and gelatin hydrolysates as well as their most recent applications.

Effects of alkaline pretreatments and acid extraction conditions on the acid-soluble collagen from grass carp (Ctenopharyngodon idella) skin.

This study investigated the effects of alkaline pretreatments and acid extraction conditions on the production of acid-soluble collagen (ASC) from grass carp skin. For alkaline pretreatment, 0.05 and 0.1M NaOH removed non-collagenous proteins without significant loss of ASC at 4, 10, 15 and 20 °C; while 0.2 and 0.5M NaOH caused significant loss of ASC, and 0.5M NaOH caused structural modification of ASC at 15 and 20 °C. For acid extraction at 4, 10, 15 and 20 °C, ASC was partly extracted by 0.1 and 0.2M acetic acid, while 0.5 and 1.0M acetic acid resulted in almost complete extraction. The processing conditions involving 0.05-0.1M NaOH for pretreatment, 0.5M acetic acid for extraction and 4-20 °C for both pretreatment and extraction, produced ASC with the structural integrity being well maintained and hence were recommended to prepare ASC from grass carp skin in practical application.

Stability of whey protein hydrolysate powders: effects of relative humidity and temperature.

Whey protein hydrolysate (WPH) is now considered as an important and special dairy protein ingredient for its nutritional and functional properties. The objectives of the present study were to investigate the effect of environmental relative humidity (RH) and storage temperature on the physicochemical stability of three WPH powders with hydrolysis degrees (DH) of 5.2%, 8.8% and 14.9%, respectively. The water sorption isotherms of the three WPH powders fitted the Guggenheim-Andersson-DeBoer model well. An increase in water content leaded to a decrease in glass transition temperature (Tg), following a linear Tg vs log water content relationship. Moreover, an increase in DH caused the decrease in Tg at the same water content. Changes in microstructure and colour occurred significantly when the WPH powders were stored at high environmental RH or temperature, especially for those with high DH.

Maillard-reaction-induced modification and aggregation of proteins and hardening of texture in protein bar model systems.

UNLABELLED: The hardening of high-protein bars causes problems in their acceptability to consumers. The objective of this study was to determine the progress of the Maillard reaction in model systems of high-protein nutritional bars containing reducing sugars, and to illustrate the influences of the Maillard reaction on the modification and aggregation of proteins and the hardening of bar matrices during storage. The progress of the Maillard reaction, glycation, and aggregation of proteins, and textural changes in bar matrices were investigated during storage at 25, 35, and 45 °C. The initial development of the Maillard reaction caused little changes in hardness; however, further storage resulted in dramatic modification of protein with formation of high-molecular-weight polymers, resulting in the hardening in texture. The replacement of reducing sugars with nonreducing ingredients such as sugar alcohols in the formula minimized the changes in texture. PRACTICAL APPLICATION: The hardening of high-protein bars causes problems in their acceptability to consumers. Maillard reaction is one of the mechanisms contributing to the hardening of bar matrix, particularly for the late stage of storage. The replacement of reducing sugars with nonreducing ingredients such as sugar alcohols in the formula will minimize the changes in texture.

Biochemical and physical changes of grass carp (Ctenopharyngodon idella) fillets stored at -3 and 0 °C.

The objective of this study was to investigate the effect of superchilling at -3 °C compared with ice storage at 0 °C on the biochemical and physical properties of grass carp fillets. Fillets stored at -3 °C showed significant changes in whiteness, drip loss and textural hardness, while changes in pH, total volatile basic nitrogen and TCA-soluble peptides were slowed down. Partial denaturation of myosin as demonstrated by differential scanning calorimetry differed between fillets stored at -3 and 0 °C in that the transition peak showed a left shoulder at -3 °C and sharpened at 0 °C. Detachments between muscle cells and formation of cracks within cells were accelerated during storage at -3 °C, and from 10 days on, clear spaces between and within cells were observed with the concurrent appearance of white spots on the surface of fillets, suggesting the formation of both extra- and intracellular large ice crystals.

Moisture-induced aggregation of alpha-lactalbumin: effects of temperature, cations, and pH.

UNLABELLED: Alpha-lactalbumin is an important dairy protein ingredient, and has been widely used in high-protein foods such as infant formula and nutritional bars for its nutritional and functional properties. The purpose of this study was to investigate the moisture-induced aggregation of alpha-lactalbumin in premixed protein dough model systems, and to illustrate the effects of temperature, cations, and pH on the progress of protein aggregation. Our results suggested that storage temperature was a critical factor for protein aggregation in model systems, and the formation of protein aggregates became faster with increases in storage temperature. Calcium significantly improved the thermal stability of alpha-lactalbumin and slowed down the formation of protein aggregates. The increases in pH accelerated the aggregation of alpha-lactalbumin. Our results also suggested that the formation of intermolecular disulfide bonds together with noncovalent interactions are the main mechanisms resulting in the moisture-induced aggregation of alpha-lactalbumin in model systems. PRACTICAL APPLICATION: Alpha-lactalbumin is an important dairy protein ingredient, and has been widely used in high-protein foods such as infant formula and nutritional bars for its nutritional and functional properties. Our results suggested low storage temperature, the presence of calcium and low pH condition can make high-protein food products containing alpha-lactalbumin more stable.