• Journal of Animal Science and Technology
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• 제58권8호
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• pp.31.1-31.8
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• 2016

Background: Plasma protein hydrolysates have been shown to possess antioxidant activity. However, no report has yet to examine the antioxidant effects of injection of plasma protein hydrolysates on meat quality. Therefore, in this study, the effects of injection of hydrolysis plasma protein solution on meat quality and storability were investigated in porcine M. longissimus lumborum. Methods: Twelve pigs were randomly selected at a commercial slaughter plant and harvested. Dissected loins were injected with one of five solutions: C- control (untreated), T1- 10 mM phosphate buffer solution (PBS), T2- 10 mM PBS with 0.01 % butylated hydroxytoluene, T3- 10 mM PBS with 5 % plasma proteins, and T4- 10 mM PBS with 5 % hydrolysis plasma proteins. Results: T3 and T4 induced greater reduction in protein content of the loin muscle than other treatments. T2 resulted in the lowest pH as well as highest cooking loss. After a storage period of 3-7 days, both lightness and redness of meat were unaffected by all injection treatments. However, yellowness was significantly elevated by treatment with T4 relative to the control. T4 also resulted in the lowest shear force (a measure of meat toughness), suggesting improvement of texture or tenderness. Further, T4 resulted in the most stable TBARS values during storage, indicating that this treatment might retard rancidity in meat. Conclusion: Injection of porcine M. longissimus lumborum with hydrolysis plasma protein solution could improve overall pork quality, including tenderness and storability.

• 한국축산식품학회지
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• 제40권2호
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• pp.172-182
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• 2020

In the present study, we determined the degree of hydrolysis (DH) of porcine blood plasma proteins, albumin, and globulin hydrolyzed by six proteases (alcalase, neutrase, flavourzyme, protamex, trypsin, and papain) for various reaction times. Moreover, antimicrobial activities of hydrolysates against five pathogenic microorganisms (Bacillus cereus, Staphylococcus aureus, Salmonella Typhimurium, Escherichia coli, and Shigella flexneri) were investigated. Alcalase, trypsin, and papain hydrolysates of the three porcine blood proteins showed higher DH values than hydrolysates produced by the other three proteases. DH of the three porcine blood proteins hydrolyzed by the six proteases failed to increase after 2 h of hydrolysis. In antimicrobial tests, hydrolysates (hydrolysis time of 2 h) showed antibacterial activity only against B. cereus. Albumin hydrolysates showed higher antimicrobial activity than globulin and plasma hydrolysates. Albumin hydrolysates obtained with flavourzyme, protamex, and trypsin showed higher antimicrobial activity than those obtained with the other three proteases.

• Journal of Applied Biological Chemistry
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• 제42권2호
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• pp.81-84
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• 1999

Blood glue was prepared to reutilize porcine blood. Plasma proteins after lyophilization were treated by addition of wood flour, sodium hydroxide, sodium silicate, and hydrated lime to make blood glue with a suitable adhesivity. Characteristics of the prepared blood glue was monitored by measuring the viscosity with time, and the relationship between degree of hydrolysis of plasma proteins by addition of various amounts of sodium hydroxide and adhesivity was studied. To prevent the emission of formaldehyde during manufacturing of plywood by blood glue, the cross-linking reaction of plasma protein with formaldehyde was also examined. Fourier transform infrared, circular dichroism, and fluorescence spectroscopy study showed that blood plasma proteins react with formaldehyde, resulting in removal of formaldehyde by cross-linking reaction.

• KSBB Journal
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• 제14권5호
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• pp.600-605
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• 1999

본 연구는 도축 폐기물인 가축혈액을 이용하여 항고혈압 기능성 식품소재로서의 angiotensin I converting enzyme 저해 펩타이드 분획을 생산하기 위한 조건과 가능성을 조사하기 위하여 수행되었다. 산업적으로 이용 가능한 단백분해효소 중 Alcalase가 혈장 원액 및 그로부터 분리된 albumin에 대하여 가장 높은 활성의 가수분해물을 생성하였다. 특히 albumin의 Alcalase 가수분해물과 이를 gel chromatography를 통새 분획하여 얻은 고활성 분획의 $IC_50$값은 각각 0.5 및 0.02 mg/mL로서 지금까지 보고된 식품단백질 유래 펩타이드 혼합물들과 비교할 때 활성이 매우 높은 것에 속함을 알 수 있었다. 또한 이 고활성 펩타이드 분획은 혈장 원액으로부터 단순한 한외여과만을 거쳐도 얻을 수 있음을 확인함으로써 산업적 실용화 가능성이 높은 공정임을 알게 되었다.

• Journal of Microbiology and Biotechnology
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• 제33권4호
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• pp.511-518
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• 2023

The use of dietary protein products has increased with interests in health promotion, and demand for sports supplements. Among various protein sources, milk protein is one of the most widely employed, given its economic and nutritional advantages. However, recent studies have revealed that milk protein undergoes fecal excretion without complete hydrolysis in the intestines. To increase protein digestibility, heating and drying were implemented; however, these methods reduce protein quality by causing denaturation, aggregation, and chemical modification of amino acids. In the present study, we observed that Lacticaseibacillus rhamnosus IDCC 3201 actively secretes proteases that hydrolyze milk proteins. Furthermore, we showed that co-administration of milk proteins and L. rhamnosus IDCC 3201 increased the digestibility and plasma concentrations of amino acids in a high-protein diet mouse model. Thus, food supplementation of L. rhamnosus IDCC 3201 can be an alternative strategy to increase the digestibility of proteins.

• BMB Reports
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• 제45권6호
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• pp.360-364
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• 2012

Uptake of circulating glucose into the cells happens via the insulin-mediated signalling pathway, which translocates the glucose transporter 4 (GLUT4) vesicles from the intracellular compartment to the plasma membrane. Rab GTPases are involved in this vesicle trafficking, where Rab GTPases-activating proteins (RabGAP) enhance the GTP to GDP hydrolysis. TBC1D4 (AS160) and TBC1D1 are functional RabGAPs in the adipocytes and the skeletonal myocytes, respectively. These proteins contain two phosphotyrosine-binding domains (PTBs) at the amino-terminus of the catalytic RabGAP domain. The second PTB has been shown to interact with the cytoplasmic region of the insulin-regulated aminopeptidase (IRAP) of the GLUT4 vesicle. In this study, we quantitatively measured the ${\sim}{\mu}M$ affinity ($K_D$) between TBC1D4 PTB and IRAP using isothermal titration calorimetry, and further showed that IRAP residues 1-49 are the major region mediating this interaction. We also demonstrated that the IRAP residues 1-15 are necessary but not sufficient for the PTB interaction.

• Bulletin of the Korean Chemical Society
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• 제34권12호
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• pp.3817-3824
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• 2013

Various separation modes in HPLC, such as anion exchange (AE), reversed-phase (RP), and affinity (AF) chromatography were examined for the separation of selenium species in human blood serum and urine. While RP- and AE-HPLC were mainly used for the separation of small molecular selenium species, double column AF-HPLC achieved the separation of selenoproteins in blood serum efficiently. Further, the effluent of AF-HPLC was enzymatically hydrolyzed and then analyzed with RP HPLC for selenoamino acid study. The versatility of the hybrid technique makes the in-depth study of selenium species possible. For quantification, post column isotope dilution (ID) with $^{78}Se$ spike was performed. ORC ICP/MS (octapole reaction cell inductively coupled plasma/mass spectrometry) was used with 4 mL $min^{-1}$ Hydrogen as reaction gas. In urine sample, inorganic selenium and SeCys were identified. In blood serum, selenoproteins GPx, SelP and SeAlb were detected and quantified. The concentration for GPx, SelP and SeAlb was $22.8{\pm}3.4\;ng\;g^{-1}$, $45.2{\pm}1.7\;ng\;g^{-1}$, and $16.1{\pm}2.2\;ng\;g^{-1}$, respectively when $^{80}Se/^{78}Se$ was used. The sum of these selenoproteins ($84.1{\pm}4.4\;ng\;g^{-1}$) agrees well with the total selenium concentration measured with the ID method of $87.0{\pm}3.0\;ng\;g^{-1}$. Enzymatic hydrolysis of each selenium proteins revealed that SeCys is the major amino acid for all three proteins and SeMet is contained in SeAlb only.