• Food Science of Animal Resources
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• v.41 no.4
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• pp.701-714
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• 2021

In this study, the microbial community succession and the protein hydrolysis of donkey meat during refrigerated (4℃) storage were investigated. 16S rDNA sequencing method was used to analyze the bacteria community structure and succession in the level of genome. Meanwhile, the volatile base nitrogen (TVB-N) was measured to evaluate the degradation level of protein. After sorting out the sequencing results, 1,274,604 clean data were obtained, which were clustered into 2,064 into operational taxonomic units (OTUs), annotated to 32 phyla and 527 genus. With the prolonging of storage time, the composition of microorganism changed greatly. At the same time, the diversity and richness of microorganism decreased and then increased. During the whole storage period, Proteobacteria was the dominant phyla, and the Photobacterium, Pseudompnas, and Acinetobacter were the dominant genus. According to correlation analysis, it was found that the abundance of these dominant bacteria was significantly positively correlated with the variation of TVB-N. And Pseudomonas might play an important role in the production of TVB-N during refrigerated storage of donkey meat. The predicted metabolic pathways, based on PICRUSt analysis, indicated that amino metabolism in refrigerated donkey meat was the main metabolic pathways. This study provides insight into the process involved in refrigerated donkey meat spoilage, which provides a foundation for the development of antibacterial preservative for donkey meat.

• BMB Reports
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• v.33 no.4
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• pp.289-293
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• 2000

Annexin I is a 37 kDa member of the annexin family of calcium-dependent phospholipid binding proteins. Annexin I plays regulatory roles in various cellular processes including cell proliferation and differentiation. Recently we found that annexin I is a heat shock protein (HSP) and displays a chaperone-like function. In this paper we investigated the function of annexin I as an ATPase using 1 to 32 amino acids deleted annexin I (${\Delta}-annexin$ I). ${\Delta}-Annexin$ I hydrolyzed ATP as determined by thin layer chromatography. The ability of ATP hydrolysis was inhibited by ADP, GTP and GDP, but not by the AMP, GMP and cAMP. In view of the ATP hydrolyzing function of HSP, the results support the function of annexin I as a HSP.

• Journal of the Korean Society of Food Science and Nutrition
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• v.1 no.1
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• pp.51-62
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• 1972

In Korea, fermented fish has been playing an important role as a preserved and flavor rich food. It is said that the digestion of fish protein is due to both action of intrinsic (autolytic enzymes) and bacterial enzymes in fish. The mass production of fermented fish has been impeded since traditional method of fermentation requires a long duration for a complete digestion. A high concentration of salt and unsanitary condition are also considered disadvantages of the old method. To improve the quality of the product and to develop mechanized process of fermentation, fermentors which have such control device as temperature, pH and agitation control system have been urgently needed. In this study, a model design of a fermentor is studied. The calculation was based on the optimum conditions for enzymatic hydrolysis of fish protein which involve temperature, pH, viscosity and other factors.

• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.5
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• pp.784-787
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• 1997

Enzymatically hydrolyzed soy sauce(eHSS) was prepared by the treatment of defatted soy flake using two types of proteases, followed by maillard reaction and formulation with some ingredients. The eHSS was mixed with fermented soy sauce(FSS) to make enzymatically hydrolyzed mixed soy sauce(eHMSS). The properties and sensory characteristics were evaluated and compared with commercially available soy sauces. The control of salt and total nitrogen contents in eHSS and eHMSS was easy, and the production of soy sauce of low salt and high protein was possible. However, the free amino acid content of eHSS was lower than FSS. due to lower degree of hydrolysis. In sensory evaluation, the eHSS have no loss taste and overall acceptance than FSS. Consequently, the eHSS and eHMSS have the potential for use with FSS to produce high quality soy sauce of low salt and high protein contents.

• Preventive Nutrition and Food Science
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• v.4 no.2
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• pp.139-144
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• 1999

Lipoprotein lipase (LPL) I san enzyme that catalyzed the hydrolysis of triacylglycerols of chylomicrons and VLDL to produce 20acylglycerols and fatty acids. The enzyme, LPL, is localized on the surface of the capillary endothelium and is widely distributed in extrahepatic tissues including heart, skeletal muscle and adipose tissue. LPL has been isolated from boving milk by affinity chromatography on heparin-separose in 2 M NaCL, 5mM barbital buffer, pH 7.4. To elucidate the lipid-binding regin, LPL was digested with trypsin and then separated by gel filtration. Lipid binding region of LPL has been investigated by recombining LPL peptides with DMPC vesicles. Proteolytic LPL fragments with DMPC were reassembled and stabilized by cholate. Lipid-binding region of LPL was identified by a PTH-automated protein sequencer, as AQQHYPVSAGYTK. The analysis of the secondary structure of the lipid-binding peptides revealed a higher probability of $\alpha$-helix structure compared to the whole LPL protein. The prediction of hydrophobicity of lipid -binding region was highly hydrophobic (-1.1) compared to LPL polypetide(-0.4).

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.2
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• pp.292-298
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• 1999

Myofibril and actomyosin were prepared from red muscle and white muscle of fresh water fish and sea water fish, and their biochemical characteristics and SDS PAGE patterns of myofibril were compared. SDS PAGE analysis showed that electrophoretic patterns of myofibril were similar be tween white muscle and red muscle, while difference of 30kDa component of myofibril was detected between fresh water fish and sea water fish. When myofibril were treated with trypsin, difference in hydrolysis of heavy chain was observed between white muscle and red muscle. In activities of Ca ATPase, Mg ATPase, EDTA ATPase and ATPase activity pH curve, myofibrillar protein from fresh water fish showed higher specific activity than those from sea water fish.

• Journal of Microbiology
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• v.41 no.1
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• pp.58-62
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• 2003

An extracellular pretense of Bacillus amyloliquefaciens S94 was purified to apparent homogeneity. The enzyme activity was strongly inhibited by general inhibitor for serine protease, PMSF, suggesting that the enzyme is a serine pretense. The purified enzyme activity was inhibited by leucine peptidase inhibitor, bestatin, suggesting that the enzyme is a leucine endopeptidase. The maximum proteolytic activity against different protein substrates occurred at pH 10, 45$^{\circ}C$ (protein substrate) and pH 8, 45$^{\circ}C$ (synthetic substrate). The purified enzyme was specific in that it readily hydrolyBed substrates with Leu or Lys residues at P$_1$ site. The pretense had characteristics of a cold-adapted protein, which was more active for the hydrolysis of synthetic substrate in the range of 15$^{\circ}C$ to 45$^{\circ}C$, specially at low temperature.

• Microbiology and Biotechnology Letters
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• v.25 no.2
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• pp.166-172
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• 1997

Aspergillus niger was selected as a strain producing the potent raw starch hydorlyzing enzyme. These experiments were conducted to investigate the conditions of the glucoa- mylase production, the purification of the enzyme, some characteristics of the purified enzyme and hydrolysis rate on various raw starches such as com, rice, potato, glutinous rice, sweet potato, wheat and barley. The optimum cultural temperature and time for the enzyme production on wheat bran medium were $30^{\circ}C$ and 96hrs, respectively. The respective addition of yeast extract and nutrient broth on wheat bran medium increased slightly the enzyme production. The enzyme was purified by ammonium sulfate fractionation and DEAE-cellulose column chromatography. The specific activity of the purified enzyme was 30.7u/mg-protein and the yield of enzyme activity was 25.8%. The purified enzyme showed a single band on polyacrylamide disc gel electrophoresis and its molecular weight was estimated to be 56,000 by SDS-polyacrylamide disc gel electrophoresis. The isoelectric point for the purified enzyme was pH3.7. The optimum temperature and pH were $65^{\circ}C$ and pH 4.0, respectively. The purified enzyme was stable in the pH range of pH 3.0-9.5 and below $45^{\circ}C$, and its thermal stability was slightly increased by the addition of $Ca^{2+}$. The purified enzyme was activated by $Co^{2+},\;Sr^{2+},\;Mn^{2+},\;Fe^{2+},\;Cu^{2+}$. Raw rice starch, raw corn starch, raw glutinous rice starch, raw sweet potato starch, raw wheat starch and raw barley starch showed more than 90% hydrolysis rate in 48hrs incubation. Even raw potato starch, most difficult to be hydrolyzed, showed 80% hydrolysis rate. The purified enzyme was identified as glucoamylase.

• BMB Reports
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• v.36 no.2
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• pp.196-200
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• 2003

Previously, we reported the biochemical properties of RGA1 that is expressed in Escherichia coli (Seo et al., 1997). The activities of RGA1 that hydrolyzes and binds guanine nucleotide were dependent on the $MgCl_2$ concentration. The steady state rate constant ($k_{cat}$) for GTP hydrolysis of RGA1 at 2 mM $MgCl_2$ was $0.0075{\pm}0.0001\;min^{-1}$. Here, we examined the effects of pH and cations on the GTPase activity. The optimum pH at 2 mM $MgCl_2$ was approximately 6.0; whereas, the pH at 2 mM $NH_4Cl$ was approximately 4.0. The result from the cation dependence on the GTPase (guanosine 5'-triphosphatase) activity of RGA1 under the same condition showed that the GTP hydrolysis rate ($k_{cat}=0.0353\;min^{-1}$) under the condition of 2mM $NH_4Cl$ at pH 4.0 was the highest. It corresponded to about 3.24-fold of the $k_{cat}$ value of $0.0109\;min^{-1}$ in the presence of 2 mM $MgCl_2$ at pH 6.0.

• Food Science of Animal Resources
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• v.30 no.6
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• pp.923-929
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• 2010

Colostral whey prepared from colostrum (pooled from first six post-partum milkings) was heated for 10 min at $100^{\circ}C$ Heated colostral whey was incubated with 1% enzymes (protein equivalent basis) for 15, 30, 60, 90, and 120 min at $50^{\circ}C$. Papain, pepsin, trypsin, and alcalase produced different degrees of hydrolysis (DH), 10.66%, 12.42%, 10.83%, and 25.31%, respectively, at an incubation time of 120 min. The SDS-PAGE reveals that significant amounts of bovine serum albumin (BSA), ${\beta}$-lactoglobulin (${\beta}$-LG), and ${\alpha}$-lactalbumin (${\alpha}$-LA) survived papain digestion. In contrast, pepsin completely removed BSA but not ${\beta}$-LG present in heated colostral whey. Alcalase completely eliminated BSA, ${\beta}$-LG, and ${\alpha}$-LA. This differential hydrolysis was confirmed by reversed-phase HPLC analysis. Using ion-exchange chromatography, fraction-1 (F-1) was obtained from alcalase hydrolysate at a NaCl gradient concentration of 0.25 M. Reversed-phase HPLC chromatograms of alcalase F-1 showed numerous small peaks, which probably indicate that a variety of new peptides were produced. Iron content of alcalase F-1 was 28.94 ppm, which was the highest among all enzyme fractions, whereas iron content of colostral whey was 36.56 ppm. Main amino acids contained in alcalase F-1 were Thr (15.45%), Glu (14.12%), and Ser (10.39%). Therefore, alcalase can be used to generate good iron-binding peptides in heated colostral whey, and the resulting iron-binding peptides could be suitable as a value-added food ingredient for food supplements.