labspec version 3.01c (HORIBA Ltd)
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labspec version 3.01c
Labspec Version 3.01c, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/labspec+version+3%2E01c/labspec+version+3+01c/pm38850642-70-16-19
Average 90 stars, based on 1 article reviews
Labspec Version 3.01c, supplied by HORIBA Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/labspec+version+3%2E01c/labspec+version+3+01c/pm38850642-70-16-19
Average 90 stars, based on 1 article reviews
labspec version 3.01c - by Bioz Stars,
2026-10
90/100 stars
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other:Article Title: The evolution of pork myosin aggregates and the relationship between aggregation modes and microstructures of O/W emulsions Article Snippet: To fabricate pork myosin nano-aggregates and investigate the effect of aggregation modes on emulsified gels, the surface charge, aggregate size, characteristic morphology, protein conformation, chemical forces and microstructures were measured at different pHs and ionic strength during the heat treatment of 75 C for 30 min.. The results showed three kinds of aggregation modes were formed, including fibril aggregation, amorphous aggregation and hydrogel aggregation, in which the characteristic morphology of myosin aggregates was fibrous strand-like, spongy, hippocampus-like and network-like, respectively.. The flexible filaments were formed with higher positive charges and larger sizes at pH 3.0, and in contrast at pH 9.0 the hydrogel was formed with higher negative charges and smaller sizes. Article Title: Structural changes and emulsion properties of goose liver proteins obtained by isoelectric solubilisation/precipitation processes Article Snippet: Structural changes and emulsion properties of proteins extracted by acid processes (ACP, pH 2.0, 2.5 and 3.0) and alkaline processes (ALP, pH 11.0, 11.5 and 12.0) were evaluated, with non-treated goose-liver (GL) paste set as the control.. Increasing contents of either reactive-sulfhydryl or surface hydrophobic groups were observed in isoelectric solubilisation/precipitation-recovered proteins (P < 0.05).. The ACP-proteins showed higher surface hydrophobicity but lower reactive-sulfhydryl content than that of ALP-proteins (P < 0.05). Article Title: Combined effects of high-pressure processing and pre-emulsified sesame oil incorporation on physical, chemical, and functional properties of reduced-fat pork batters Article Snippet: Spectra were smoothed, baselines corrected and normalized against the phenylalanine band at 1003 cm −1 ( ) using Article Title: Effects of high-intensity ultrasound on physicochemical and gel properties of myofibrillar proteins from the bay scallop ( Argopecten irradians ) Article Snippet: The phenylalanine (Phe) ν_ring band at 1003 cm −1 was smoothed, baseline corrected, and normalized using Article Title: Emulsion‐forming properties of heat‐induced pork myofibrillar protein affected by NaCl Article Snippet: The emulsification characteristics of myofibrillar proteins (MPs) with different NaCl concentrations also affect the quality of meat products after cooking.. We investigated the effects of heating (100 °C) on the solubility, emulsifying activity, and conformational and environmental changes of MPs prepared with different NaCl concentrations.. Emulsifying activity increased with increasing NaCl prior to heating, but there was no significant effect after heating. Article Title: Effects of high-intensity ultrasound on physicochemical and gel properties of myofibrillar proteins from the bay scallop (Argopecten irradians). Article Snippet: The phenylalanine (Phe) ν_ring band at 1003 cm− 1 was smoothed, baseline corrected, and normalized using Article Title: Effects of regenerated cellulose fiber on the characteristics of myofibrillar protein gels. Article Snippet: The study investigated the role of regenerated cellulose (RC) fiber (0, 5 g, 10 g, 15 g and 20 g/100 g) on water holding capacity (WHC), texture, dynamic rheological, secondary structures and microstructure of myofibrillar protein (MP) gels.. It was found that the gel WHC and texture properties were enhanced with increased RC fiber.. The rheological results indicated that RC fiber did not destroy the normal cross-link of MP, but enhanced the viscoelasticity. |