scholarly journals Comparative effects of dry-aging and wet-aging on physicochemical properties and digestibility of Hanwoo beef

2020 ◽  
Vol 33 (3) ◽  
pp. 501-505 ◽  
Author(s):  
Ji-Han Kim ◽  
Tae-Kyung Kim ◽  
Dong-Min Shin ◽  
Hyun-Wook Kim ◽  
Young-Boong Kim ◽  
...  

Objective: The purpose of this study was to investigate the effects of aging methods (AM) i.e. dry-aging (DA) and wet-aging (WA) on the physicochemical properties and in vitro digestibility of proteins in beef short loin.Methods: Short loins (M. longissmus lumborum), were trimmed and boned-out on the fifth day postmortem, from a total of 18 Hanwoo, which were purchased from a commercial slaughterhouse. Short loins were separated randomly grouped into one of the three treatments: control, WA (1°C, 7 days), and DA (1°C, 0.5 m/s, 85% relative humidity [RH], 30 days).Results: Dry-aged beef (DAB) exhibited higher pH, water holding capacity (WHC), myofibrillar fragmentation index (MFI), and digestibility, however lower lightness, redness, and yellowness values, cooking loss, and shear force (SF), than those of wet-aged beef (WAB) (p<0.05). The myosin light chain band intensity of DAB was higher than that of control and WAB in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The in vitro digestibility of aged beef was highly (p<0.001) correlated to physicochemical properties except WHC. The correlation coefficient between AMs and WHC was higher than that between AM and SF (p<0.05) or MFI (p<0.001). A high correlation was observed between SF and MFI (p<0.001).Conclusion: Thus, we believe that DAB is more advantageous than WAB owing to its high digestibility and WHC and low SF.

Foods ◽  
2019 ◽  
Vol 8 (12) ◽  
pp. 594 ◽  
Author(s):  
Tian Tian ◽  
Fei Teng ◽  
Shuang Zhang ◽  
Baokun Qi ◽  
Changling Wu ◽  
...  

Use of soy protein isolate (SPI) as the encapsulating material in emulsions is uncommon due to its low solubility and emulsification potential. The aim of this study was to improve these properties of SPI via heat treatment-induced modifications. We modified SPI under various heating conditions and demonstrated the relationship between structure and in vitro digestibility in simulated gastric fluid by means of Sodium Dodecyl Sulphide-Polyacrylamide Gel Electrophoresis (SDS-PAGE) and Raman spectroscopy. It was found that the degree of hydrolysis (DH) of SPI increased and then decreased upon increasing exposure to heat. Different subunits of conglycinin were digested and degraded by pepsin. Heat treatment improved digestion characteristics that would reduce e the unnecessary loss of protein, offering potential for the efficient delivery of nutrients in nanoemulsions. These results could have significant relevance for research groups that are interested in the biological interactions and activity of functional SPI.


2018 ◽  
Vol 2 (3) ◽  
pp. 70
Author(s):  
Benard O. Oloo ◽  
Mahungu S. ◽  
Kahi A. ◽  
Eric Amonsou

<p><em>The aim of this study was to evaluate the effect of the cluster ecotype and the part of chicken on nutritional composition, and functionality of sarcoplasmic and myofibrillar proteins that are most relevant to the technological features of chicken meat. Over 50 chickens from each ecotype cluster purchased, slaughtered and the meat stored under refrigeration at -20<sup>o</sup>C and later on transferred in cooler box on ice and flown to South Africa, at the Durban University of Technology. Protein fractions were extracted with a cocktail of Sodium Chloride buffer (50mM NaCl, 50mM Tris HCl; 75mM DTT and 1mM EDTA at pH 7) and quantified by Bradford method. One dimensional Sodium Dodecyl Polyacrylamide Gel Electrophoresis (SDS PAGE) was applied to separate protein fractions. Emulsifying capacity, emulsifying stability, solubility, and in vitro digestibility were determined on the total protein isolates. Significant differences in band expressions were recorded for the myofibrillar and the sarcoplasmic proteins. The three ecotypes had high quality proteins with all the limiting and essential amino acids at concentrations higher than FAO/WHO recommended daily allowance for adults and children. Distinct protein bands at larger molecular weight proteins &gt;100 kDa, corresponding to Myosin Heavy Chain, medium fractions 75 kDa and 45 kDa and even lower molecular weight fraction &lt;25 kDa were present in the chicken breast and the thighs. It concludes that Indigenous chicken protein isolates’ nutritional and functional properties are affected by part of chicken and ecotype clusters. </em></p>


2018 ◽  
Vol 18 (1) ◽  
pp. 10-15
Author(s):  
Wang Yi-Wei ◽  
He Yong-Zhao ◽  
An Feng-Ping ◽  
Huang Qun ◽  
Zeng Feng ◽  
...  

In this study, Chinese yam starch-water suspension (8%) were subjected to high-pressure homogenization (HPH) at 100 MPa for increasing cycle numbers, and its effect of on the physicochemical properties of the starch was investigated. Results of the polarizing microscope observations showed that the starch granules were disrupted (i.e. greater breakdown value) after HPH treatment, followed by a decrease in cross polarization. After three HPH cycles, the crystallinity of starch decreased, while the crystal type remained unaltered. Meanwhile, the contents of rapidly digestible starch and slowly digestible starch were increased. On the contrary, resistant starch content was decreased. Our results indicate that HPH treatment resulted in reduction of starch crystallinity and increase of starch digestibility.


2021 ◽  
pp. 2100102
Author(s):  
Shuyu Jia ◽  
Bin Yu ◽  
Haibo Zhao ◽  
Haiteng Tao ◽  
Pengfei Liu ◽  
...  

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Umar Shah ◽  
Deepak Dwivedi ◽  
Mark Hackett ◽  
Hani Al-Salami ◽  
Ranjeet P. Utikar ◽  
...  

AbstractKafirin, the hydrophobic prolamin storage protein in sorghum grain is enriched when the grain is used for bioethanol production to give dried distillers grain with solubles (DGGS) as a by-product. There is great interest in DDGS kafirin as a new source for biomaterials. There is however a lack of fundamental understanding of how the physicochemical properties of DDGS kafirin having been exposed to the high temperature conditions during ethanol production, compare to kafirin made directly from the grain. An understanding of these properties is required to catalyse the utilisation of DDGS kafirin for biomaterial applications. The aim of this study was to extract kafirin directly from sorghum grain and from DDGS derived from the same grain and, then perform a comparative investigation of the physicochemical properties of these kafirins in terms of: polypeptide profile by sodium-dodecyl sulphate polyacrylamide gel electrophoresis; secondary structure by Fourier transform infra-red spectroscopy and x-ray diffraction, self-assembly behaviour by small-angle x-ray scattering, surface morphology by scanning electron microscopy and surface chemical properties by energy dispersive x-ray spectroscopy. DDGS kafirin was found to have very similar polypeptide profile as grain kafirin but contained altered secondary structure with increased levels of β-sheets. The structure morphology showed surface fractals and surface elemental composition suggesting enhanced reactivity with possibility to endow interfacial wettability. These properties of DDGS kafirin may provide it with unique functionality and thus open up opportunities for it to be used as a novel food grade biomaterial.


2021 ◽  
Author(s):  
Huishan Shen ◽  
Xiangzhen Ge ◽  
Bo Zhang ◽  
Chunyan Su ◽  
Qian Zhang ◽  
...  

Non-thermal plasma is an emerging and effective starch modification technology. In this paper, plasma pretreatment was used to modify the citrate naked barley starch for enhancing the accessibility of citric...


1982 ◽  
Vol 2 (4) ◽  
pp. 412-425 ◽  
Author(s):  
S I Reed ◽  
J Ferguson ◽  
J C Groppe

The CDC28 gene was subcloned from a plasmid containing a 6.5-kilobase-pair segment of Saccharomyces cerevisiae DNA YRp7(CDC28-3) by partial digestion with Sau3A and insertion of the resulting fragments into the BamHI sites of YRp7 and pRC1. Recombinant plasmids were obtained containing inserts of 4.4 and 3.1 kilobase pairs which were capable of complementing a cdc28(ts) mutation. R-loop analysis indicated that each yeast insert contained two RNA coding regions of about 0.8 and 1.0 kilobase pairs, respectively. In vitro mutagenesis experiments suggested that the smaller coding region corresponded to the CDC28 gene. When cellular polyadenylic acid-containing RNA, separated by agarose gel electrophoresis after denaturation with glyoxal and transferred to nitrocellulose membrane, was reacted with labeled DNA from the smaller coding region, and RNA species of about 1 kilobase in length was detected. Presumably, the discrepancy in size between the R-loop and electrophoretic determinations is due to a segment of polyadenylic acid which is excluded from the R-loops. By using hybridization of the histone H2B mRNAs to an appropriate probe as a previously determined standards, it was possible to estimate the number of CDC28 mRNA copies per haploid cell as between 6 and 12 molecules. Hybrid release translation performed on the CDC29 mRNA directed the synthesis of a polypeptide of 27,000 daltons, as determined by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. This polypeptide was not synthesized when mRNA prepared from a cdc28 nonsense mutant was translated in a parallel fashion. However, if the RNA from a cell containing the CDC28 gene on a plasmid maintained at a high copy number was translated, the amount of in vitro product was amplified fivefold.


1994 ◽  
Vol 14 (9) ◽  
pp. 6164-6170
Author(s):  
P P Sadhale ◽  
N A Woychik

We identified a partially sequenced Saccharomyces cerevisiae gene which encodes a protein related to the S. cerevisiae RNA polymerase II subunit, RPB7. Several lines of evidence suggest that this related gene, YKL1, encodes the RNA polymerase III subunit C25. C25, like RPB7, is present in submolar ratios, easily dissociates from the enzyme, is essential for cell growth and viability, but is not required in certain transcription assays in vitro. YKL1 has ABF-1 and PAC upstream sequences often present in RNA polymerase subunit genes. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis mobility of the YKL1 gene product is equivalent to that of the RNA polymerase III subunit C25. Finally, a C25 conditional mutant grown at the nonpermissive temperature synthesizes tRNA at reduced rates relative to 5.8S rRNA, a hallmark of all characterized RNA polymerase III mutants.


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