Toshihide Nishimura

Effect of fat content on sensory characteristics of marbled beef from Japanese Black steers

To analyze the sensory characteristics of meat samples with a crude fat content between 23.8% and 48.6% taken from 34 Japanese Black steers, we grilled the meat and subjected it to analytical sensory evaluation. We also measured the amounts of moisture, protein, nucleic acid and glutamic acid. An increase in crude fat content increased the tenderness, juiciness, and fattiness in the meat quality evaluation. An increase in crude fat content reduced the crude protein and moisture contents; it also slightly reduced the nucleic acid and glutamic acid contents, although when the reductions in these umami components were assessed relative to the moisture content they changed little. Increasing the fat content up to a certain point greatly enhanced the umami intensity and beef flavor intensity in the meat quality evaluation and raised the overall evaluation score; the peak of the appropriate crude fat content for these purposes was about 36%.

Changes in taste compounds, breaking properties, and sensory attributes during dry aging of beef from Japanese black cattle

Analysis of the quality of highly marbled beef during dry aging for 60days after slaughter showed that the changes in some qualities differed from those of conventional meat. The tenderness of these meats did not change during aging for 50days but then gradually increased until day 60. The juiciness of these meats, as determined by sensory evaluation, did not change during aging for 60days, except for a decrease on day 20. The umami intensity of these meats in the sensory evaluation and the value calculated by Glu and IMP quantification were highest on day 40. This high umami intensity was induced by the synergistic effect of umami compounds such as Glu and IMP. These results for tenderness, juiciness, umami intensity, and flavor intensity suggested that the best duration of dry aging for highly marbled beef was 40days.

Characterization of the key aroma compounds in beef extract using aroma extract dilution analysis.

Aroma extract dilution analysis (AEDA) of an ether extract prepared from beef extract (BE) and subsequent identification experiments led to the determination of seven aroma-active compounds in the flavor dilution (FD) factor range of 32-128. Omission experiments to select the most aroma-active compounds from the seven aroma compounds suggested that 2,3,5-trimethyl pyrazine, 1-octen-3-ol, 3-methylbutanoic acid, and 4-hydroxy-2,5-dimethyl-3(2H)-furanone were the main active compounds contributing to the aroma of BE. Aroma recombination, addition, and omission experiments of the four aroma compounds in taste-reconstituted BE showed that each compound had an individual aroma profile. A comparison of the overall aroma between this recombination mixture and BE showed a high similarity, suggesting that the key aroma compounds had been identified successfully.

Phytosterols in onion contribute to a sensation of lingering of aroma, a koku attribute.

We aimed to examine the substance in a precipitate of heat-treated onion concentrate (HOC) that contributes to a sensation of lingering of aroma, a koku attribute induced by the sensing of richness and persistence in terms of taste, aroma and texture. Adding precipitate, separated from HOC, to consommé enhanced the lingering sensation of aroma in the consommé more than adding the supernatant from HOC. After the precipitate was washed with hot water and ethanol its enhancing effect disappeared. Analysis of the HOC precipitate showed that it contained phytosterols, such as beta-sitosterol and stigmasterol. Tests of binding to aroma compounds showed that both sterols, as well as the washed precipitate, were able to bind methyl propyl disulfide and N-hexanal. Thus phytosterols in the HOC precipitate seemed to bind and hold the aroma compounds and gradually release them, inducing a lingering sensation of aroma under the koku concept during consumption.

Antioxidative Properties of Peptides Obtained from Porcine Myofibrillar Proteins by a Protease Treatment in an Fe (II)-Induced Aqueous Lipid Peroxidation System

The porcine myofibrillar protein hydrolysate obtained by a papain treatment showed antioxidative activity in a system of linolenic acid peroxidation induced by Fe2+. The five peptides, DSGVT, IEAEGE, DAQEKLE, EELDNALN, and VPSIDDQEELM, have been characterized as antioxidative peptides (Saiga et al., J. Agric. Food Chem., 51, 3661–3667 (2003)). These peptides were synthesized and their antioxidative activity evaluated. The antioxidative activity of four peptides, excluding DSGVT, was confirmed by their addition at 0.1% to the peroxidation system. To clarify the mechanism for the antioxidative activity of these peptides, their short peptides with amino acid deletions at the C- or N-termini were synthesized. The antioxidative activity gradually decreased with decreasing peptide length. Replacing the charged amino acids in these peptide sequences with Ala also affected their antioxidative activity. We hypothesize that the anions from acidic amino acids and the cations from iron interacted with each other and inactivated the pro-oxidant, Fe (II).

Characterization of the key aroma compounds in pork soup stock by using an aroma extract dilution analysis

The aroma extract dilution analysis of an extract prepared from pork stock and subsequent experiments led to the identification of 15 aroma-active compounds in the flavor dilution factor range of 64–2048. Omission experiments to select the most aroma-active compounds from the 15 odor compounds suggested acetol, octanoic acid, δ-decalactone, and decanoic acid as the main active compounds contributing to the aroma of pork stock. Aroma recombination, addition, and omission experiments of these four aroma compounds in taste-reconstituted pork stock showed that each compound had an individual aroma profile. A comparison of the overall aroma between this recombined mixture and pork stock showed strong similarity, suggesting that the key aroma compounds had been successfully identified. Graphical Abstract Most aroma-active compounds contributing to the aroma of clear type pork stock detected by AEDA and subsequent omission and addition experiments.

Actions of cathepsins on troponin T during postmortem aging of porcine muscle

In this study, we examined the contribution of the cathepsins (cathepsin D and crude cathepsins containing cathepsins B and L) to troponin T degradation during postmortem aging. The action of cathepsin D on troponin T was examined at various pHs (pH 4.0-6.5). The degradation of intact troponin T was observed at pH 4.0, but not observed at pH 5.5 and 6.5. As a result of the degradation of troponin T, the 30 kDa fragment was not generated in any pH condition. The action of the crude cathepsins on troponin T was also examined at various pHs (pH 4.0-6.5). The intact troponin T was degraded at pH 4.0 and the 30 kDa fragments were observed. These 30 kDa fragments disappeared during further incubation. On the other hand, at pH 5.5 and 6.5, the intact troponin T was degraded and the 30 kDa fragment was accumulated. These results suggested that the cathepsin D scarcely contributed to the degradation of troponin T during postmortem aging, but crude cathepsins containing cathepsins B and L were partially involved in the degradation of troponin T and the generation of 30 kDa fragments.

Purification and characterization of porcine skeletal muscle aminopeptidase T, a novel metallopeptidase homologous to leukotriene A4 hydrolase.

A novel aminopeptidase, Aminopeptidase T (APase T), was purified from porcine skeletal muscle following successive column chromatography: twice on DEAE-cellulose, hydroxyapatite, and Sephacryl S-200 HR using Leu-β-naphthylamide (LeuNap) as a substrate. The molecular mass of the enzyme was 69 kDa on SDS–PAGE. The optimum pH towards LeuNap of the enzyme was about 7. The enzyme activity was strongly inhibited by bestatin and was negatively affected by ethylenediaminetetraacetic acid (EDTA). Chlorine-activated APase T liberated Leu, Ala, Met, Pro, and Arg from Nap derivatives. The APase T gene consisted of an ORF of 1,836 bp encoding a protein of 611 amino acid residues. The APase T was highly homologous to bovine, human, and mouse Leukotriene A4 hydrolase (LTA4H), a bifunctional enzyme which exhibits APase and epoxide hydrolase activity.