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    Physico-chemical and Textural Properties of 3D Printed Plant-based and Hybrid Soft Meat Analogs
    (Springer Science+Business Media, LLC, part of Springer Nature, 2023-06) Wang T; Kaur L; Beniwal AS; Furuhata Y; Aoyama H; Singh J
    This study investigated the physico-chemical and textural properties of 3D-printed pea protein-only and pea protein-chicken-based hybrid meat analogs. Both pea protein isolate (PPI)-only and hybrid cooked meat analogs had a similar moisture content of approximately 70%, which was similar to that of chicken mince. However, the protein content increased significantly with the amount of chicken in the hybrid paste undergoing 3D printing and cooking. Significant differences were observed in the hardness values of the non-printed cooked pastes and the 3D printed cooked counterparts, suggesting that the 3D printing process reduces the hardness of the samples and is a suitable method to produce a soft meal, and has significant potential in elderly health care. Scanning electron microscopy (SEM) revealed that adding chicken to the plant protein matrix led to better fiber formation. PPI itself was not able to form any fibers merely by 3D printing and cooking in boiling water. Protein-protein interactions were also studied through the protein solubility test, which indicated that hydrogen bonding was the major bonding that contributed to the structure formation in cooked printed meat analogs. In addition, disulfide bonding was correlated with improved fibrous structures, as observed through SEM.
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    Adhesion of salmonella species and Escherichia coli to collagen fibres of chicken connective tissue : a thesis submitted in partial fulfilment of the requirements for the degree of Master of Science
    (Massey University, 1984) Campbell, Susan
    This thesis describes an investigation of some factors affecting attachment of salmonellae and Escherichia coli to collagen fibres of poultry breast muscle fascie. Direct microscopic techniques were used in conjunction with standard microbiological methods as a means of examining the attachment process. All strains of salmonellae tested, fimbriate Escherichia coli and a strain of Campylobacter coli adhered to collagen when muscle fascie was immersed in water containing cells of the appropriate test culture. Adhesion was dependent on water induced changes in fascie structure and was inhibited or reversed by addition of sodium chloride to the suspending medium. Capsular glycocalyx also prevented attachment of these bacteria to collagen fibres. TEM studies indicated attached cells were held to the collagen by acidic mucopolysaccharides (or glycosaminoglycans) associated with the intercollagen fibre matrix of fascie. Subsequent studies showed hyaluronic acid (a predominant glycosaminoglycan associated with collagenous tissue) could inhibit attachment of selected strains of Salmonella and E. coli, but this ingibition could be reversed by hyaluronidase. Chondroitin-sulphate, a related glycosaminoglycan, only inhibited attachment of E. coli strains. This evidence implicated hyaluronate as a key factor in the attachment process. Since only fimbriate E. coli could bind significant amounts of hyaluronic acid, it is usggested these bacteria may bind directly to tissue glyclsaminoglycans. Salmonellae, however, apparently require an additional bridging compoung (possibly a protein) to mediate adhesion to collagen fibres.