• Asian-Australasian Journal of Animal Sciences
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• v.16 no.3
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• pp.417-424
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• 2003

Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, $\alpha$-chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and $\alpha$-chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by $\alpha$-chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.

• Korean Journal of Veterinary Research
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• v.44 no.2
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• pp.269-277
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• 2004

Trichinella spiralis is one of the important zoonotic parasites with a wide variety of vertebrates hosts in nature. The purpose of this study were to analyze ESP(Excretory-Secretory Protein) antigen, to evaluate ELISA for the serological diagnosis of Trichinosis, and to survey T. spiralis infection in finishing pigs using the pepsin digestion method and ELISA in Korea. In the analysis of ESP antigen by SDS-PAGE and Western blot, 4 major bands (70, 55, 52.6, and 49 kDa) were revealed from the ESP antigen. Predilection sites of T. spiralis were the diaphragm, the tongue, masseter muscles, intercostal muscle, and hindlimb in orders in the experimentally infected rats. Sera from 581 swine were tested by ELISA with ESP antigen. The 54 (9.3%) sera were suspected as positive reactors, however, these 54 sera were determined as false positives by the use of Western blotting. This study demonstrated that the ELISA was not suitable for the examination of T. spiralis in pork. The diaphragm muscle samples of 251 finishing pigs were tested by the method of pepsin-digestion for the presence of Trichinella larvae, however, T. spiralis was not detected from the samples. We could not find out T. spiralis infection in pig in Korea pork.

• Current Research on Agriculture and Life Sciences
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• v.31 no.2
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• pp.108-112
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• 2013

Nuts are one of the most common sources of allergies in individuals of all ages. In order for a particular protein to render an allergic reaction, it must resist proteolytic digestion by intestinal enzymes. In this study, three well-known allergenic nuts, almonds, cashew nuts, and peanuts, were used as samples, and enzyme digestion with Bacillus protease and porcine pepsin was tested. A proteomic approach using two-dimensional gel electrophoresis and an MS/MS analysis was applied to visualize and identify the proteins that were resistant to enzyme digestion. Among the 150 protein spots tested, 42 proteins were assigned functions. Due to the lack of genomic databases, 41% of the identified proteins were grouped as hypothetical. However, 12% of them were well-known allergens, including AraH. The remainder were grouped as storage, enzymes, and binding proteins.

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.2
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• pp.438-443
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• 1999

A livetin solution(LS) containing yolk immunoglobulins(IgY) was separated by treating the egg yolk with natural gum, carrageenan. Carrageenan has been used as a food ingredient. Relative absorbance of IgY LS after proteolysis was investigated. IgY LS was fairly stable to pepsin digestion at pH 3.0. However, IgY LS appeared to be susceptible to pepsin digestion at pH 2.0, showing 18% of relative absorbance and complete breakdown H chain after 30 min exposure. Relative absorbance of IgY LS was considerably high after exposure to trypsin and chymotrypsin for 8 hr. IgY LS showed especially good stability to chymotrypsin digestion.

• Korean Journal of Soil Science and Fertilizer
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• v.38 no.5
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• pp.253-258
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• 2005

It is necessary to determine a nitrogen supplying capacity (NSC) of soil for sustainable agriculture. NSC has been decided by directly detecting N mineralization potential (NMP) and inorganic nitrogen or by indirectly approximating from organic matter and chemical properties of soil. NMP is best method for NSC but it takes long period. A study was conducted to find a short-term incubation method using pepsin through 1) determining NMP of 3 upland and 3 paddy soils, 2) establishing analytical condition of pepsin digestion by comparing to NMP, 3) validating with relations to N requirements for maximum yield of rice. NMPs of 6 soils were ranges from $63mg\;N\;kg^{-1}$ to $156mg\;N\;kg^{-1}$. The pepsin digestion method of soil nitrogen was established by determining amino nitrogen from digesting 5 g of soil for 30 minutes by 0.02% pepsin. This method was so highly correlated with a maximum rate of nitrogen fertilizer that it could be used for determining NSC in paddy soil.

• Asian-Australasian Journal of Animal Sciences
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• v.13 no.3
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• pp.317-322
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• 2000

In situ and in vivo digestion trials were conducted to determine the degradation of dry matter (DM), crude protein (CP) and effective protein degtadability (EPD), and digestibility of nutrients of Hazelnut kernel oil meal (HKOM), and effects of HKOM on nitrogen (N) balance. In the in situ study, nylon bag were suspended in the rumen of 3 Karayaka rams to estimate protected protein. Protein sources were analyzed for pepsin soluble protein (PSP) using a Pepsin Digestion Method. In the digestion trials, 4 Karayaka rams (36 mo.) were used in a $4{\times}4$ Latin square to evaluate the digestibility of nutrients and N retention to measure effects of diets containing HKOM, soybean meal (SBM) corn gluten meal (CGM) and urea (U). The degradability of DM and CP, and PSP content of HKOM were lower (p>0.05) than that of SBM, but higher (p<0.001) than that of CGM. EPD of HKOM was higher (p<0.01) than that of SBM or CGM. The apparent digestion coefficients of organic matter and CP for HKOM were lower than for SBM, but higher than for CGM. N retention of HKOM was higher than that of SBM and lower than that of CGM (p>0.05). In conclusion, these data may indicate that the HKOM is a high digestible feed source with a value between SBM and CGM.

• Asian-Australasian Journal of Animal Sciences
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• v.20 no.12
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• pp.1849-1857
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• 2007

The experiment was carried out using fistulated multiparous Holstein Friesian crossbred (75% Holstein Friesian and 25% Red Sindhi) dairy cows in their dry period fed on untreated rice straw to evaluate the nutritive value of local protein feed resources using the in sacco method and in vitro pepsin-pancreatin digestion. Experimental feeds were cottonseed meal (CSM); soybean meal (SBM); dried brewery's grains (DBG); palm kernel meal (PSM); cassava hay (CH); leucaena leaf meal (LLM). Each feedstuff was weighed into duplicate nylon bags and incubated in each of the two rumen fistulated cows for 0, 2, 4, 8, 16, 24, and 48 h. Rumen feed residues from bags of 16 h incubation were used for estimation of lower gut digestibility by the technique of in vitro pepsin-pancreatin digestion. Ruminal ammonia-nitrogen ($NH_3-N$) concentrations did not differ between treatments or time with a mean of 5.5 mg%. Effective degradability of DM of CSM, SBM, DBG, PSM, CH and LLM were 41.9, 56.1, 30.8, 47.0, 41.1 and 47.5%, respectively. Effective degradabilities of the CP in feedstuffs were 49.6, 59.2, 40.9, 33.5, 47.3 and 65.0% for the respective feedstuffs. The CP in vitro pepsin-pancreatin digestibility as ranked from the highest to the lowest were SBM, CSM, LLM, CH, DBG, PSM, respectively. The intestinal and total tract digestion of feedstuffs in the current study were relatively lower than that obtained from previous literature. The results of this study indicate that SBM and LLM were highly degradable in the rumen, while CH, CSM and DBG were less degradable and, hence resulted in higher rumen undegradable protein. Soybean meal and LLM could be used to improve rumen ecology whilst CH, CSM and DBG could be used as rumen by-pass protein for ruminant feeding in the tropics.

• Korean Journal of Poultry Science
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• v.11 no.1
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• pp.13-17
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• 1984

Protein digestibitlities of hydrolyzed cattle skin meals were examined at a constant pepsin-MC$\ell$ concentration (0.2%) for varying lengths of incubation time (from 4 to 20 hours) and at varying concentrations of pepsin-HC$\ell$ (from 0.0125 to 0.2%) for 16 hours at 45$^{\circ}C$. The results are summarized as follows: 1. Protein digestibilities of hydrolyzed cattle skin meals in 0.2% pepsin-HCl were 66.31%, 80.69%, 83.72%, 84.65% and 81.45% for 4, 8, 12, 16 and 20 hours incubation, respectively. Protein digestibilities were maintained above 80% for 8-hour incubation and were increasing incubation time. 2. Protein digestibilities of hydrolyzed cattle skin meal incubated for 16 hours at 0.2%, 0.1%, 0.05%, 0.025% and 0.0125% pepsin-HC$\ell$ solution were 85.10%, 82.08%, 76.18%, 74.67% and 64.82%, respectively. Protein digestibilities were decreased with decreasing pepsin concentration.

• Food Science and Biotechnology
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• v.16 no.3
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• pp.493-495
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• 2007

In this study, the acrylamide contents of foods were estimated via liquid chromatography (LC)/mass spectrometry (MS)/MS after the food matrix constituents had been degraded with digestive enzymes (i.e., pepsin and pancreatin) and extracted with water. The quantities of acrylamide released from samples of cereal, potato chips, peanuts, and coffee were $62{\pm}5.1,\;970,\;106{\pm}20$, and 890 ppb, respectively. No acrylamide was detected in samples of soybean curd (tofu), fish cake, and ham. Compared to the amounts of acrylamide detected after extraction with water only, we noted no significant differences in the soybean curd, fish cake, potato chip, ham, and coffee samples. However, the quantities of acrylamide released from the cereal and peanut samples were approximately 2-fold larger following pretreatment with the digestive enzymes. This study presents a new in vitro enzymatic digestion method which allows for a more accurate estimation of the acrylamide contents of foods.

• Journal of Animal Science and Technology
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• v.49 no.1
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• pp.129-136
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• 2007

This study was performed to determine the protein profiles using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Angiotensin-I-converting enzyme(ACE) inhibitory activity (IC50) as affected by the various meat cuts, digestion times with pepsin. Hydrolysates having the protein concentration of 10 ug/mL had approximately 36∼39% ACE inhibitory activities, regardless of meat cut and digestion time. Protein concentration and ACE inhibitory activity of the diluted hydrolysate increased after 1-hr digestion. In original hydrolysates, ACE inhibitory activities of loin had higher than those of round (P<0.05). In addition, non-heated hydrolysates had higher ACE inhibitory activities than heated counterparts. When myosin B was digested by pepsin more than 1 hr, improved ACE inhibitory activities were observed as compared to the non-digested control.