• Preventive Nutrition and Food Science
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• v.5 no.4
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• pp.179-183
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• 2000

$\beta$-1,4-Mannotriose was prepared b he enzymatic hydrolysis of white copra meal (WCM) and the subsequent elimination of monosaccharides from the resultant hydrolysate with a yeast. The enzyme system from sunflower seed hydrolyzed WCM and produced monosaccharides and $\beta$-1,4-mannotriose without other oligomers at the final stage of the reaction. WCM(50g) was hydrolyzed at 5$0^{\circ}C$ and pH 4.5 for 24 hr with crude enzyme solution (500 mL) from sunflower seed. By the elimination of monosaccharides from the hydrolysis products with a yeast (Candida glaebosa), 8.1 g of crystalline mannotriose was obtained without the use of chromatographic techniques. After 48hr of yeast cultivation, the total sugar content decreased from 4.6% to 3.5%, whereas the average degree of polymerization increased from 2.3 to 3.1.

• The Korean Journal of Food And Nutrition
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• v.9 no.2
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• pp.167-175
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• 1996

This studies were conducted to select optimal enzyme that produced hydrolysate from soybean, and to evaluated functionality of hydrolysate. Soybean powder was suspended with water and hydrolyzed by seven commercial proteases. Hydrolysate produced with protease from Bacillus subtilis showed the highest inhibition effect on the activity of angiotension converting enzyme(ACE), and the condition of enzymatic hydrolysis was 5cA substrate concentration, 0. l% enzyme concentration, 4 hour hydrolysis time. Under above optimum condition, soybean was hydrolyzed with protease from Bacillus subtilis yielding a DH (degree of hydrolysis) of about 49%. Hyrophobicity of hydrolysate was not correlated with the inhibition effect on ACE activity. The functionality of hydrolysate was significantly influenced by pH. Solubility of hydrolysate at alkali solution was greater than that at acidic solution.

• Clean Technology
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• v.19 no.4
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• pp.393-400
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• 2013

In this study, Polyethylene wax, which was produced in manufacturing process of high density polyethylene was grafted with maleic anhydride (MAH). The influences of reaction parameters on the graft polymerization as well as the effect of hydrolysis of the anhydride functions were investigated. The results show that the grafting degree increased and conversion of maleic anhydride decreased with an increase in MAH monomer content. This means the highest grafting efficiency for the reaction can be met when MAH monomer content is about 15 wt%. DCP (dicumyl peroxide) and DTBP (di-tert-butyl peroxide) have been used as the initiator and the highest yield of grafting was obtained when the initiator content is about 0.5 wt%. However, It can be seen that the gel content values of this polyethylene wax grafted MAH were below 2%. It was also observed that the grafting degree increased with an increase in reaction temperature and the maximum value was reached 2 hours later. Although MAH functions grafted onto polyethylene wax were mainly in the carboxylic acid forms, some anhydride form of MAH appeared in over 5% of grafting degree. As a result of hydrolysis reaction, it was observed that the conversion of anhydride group into carboxylic acid group was reached up to 10%.

• Food Science of Animal Resources
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• v.40 no.2
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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.

• Microbiology and Biotechnology Letters
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• v.32 no.4
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• pp.347-351
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• 2004

Hydrolysis of manno-oligosaccharides and galactomannan was studied with the purified Bacillus subtilis WL-7 mannanase from recombinant Eschericoli. The predominant products of hydrolysis were mannose, mannobiose and mannotriose. The enzyme could hydrolyze $\beta$-1 A-linked manno-oligosaccharides larger than mannobiose, but was not active on mannobiose. When the mannanase hydrolyzed manno-oligo saccharides of degree of polymerization(DP) 4-6, it was more active on the substrate of higher DP. Based on analysis of transient reaction products by TLC, the enzyme was found to have a preference for internal $\beta$-IA-mannosidic linkages, which are the central mannosidic bond of mannotetraose and the two middle mannosidic bonds of mannopentaose. The $\beta$-l A-mannosidic bonds situated at the second and fourth positions from the nonreducing end of mannohexaose were preferenhydrolyzed by the mannanase. Locust bean gum(LBG) was enzymatically hydrolyzed with higher efficiency than guar gum, resulting that amount of reducing sugars was liberated more efficiently from LBG than guar gum with same activity of mannanase.

• Korean Journal of Food Science and Technology
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• v.22 no.3
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• pp.234-240
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• 1990

Attempts have been made to optimize the hydrolysis conditions of the oyster and the mussel by the commercial proteolytic enzymes. Raw materials were digested with seven different commercial enzymes, and their quality parameters measured in terms of degree of hydrolysis and content of free amino nitrogen, nucleic acid-related substances. and free amino acids as well as sensory evaluation of optimization of their hydrolysis conditions. As a result, following enzymes have been disclosed as effective for enzymatic digestion: MKC-HT proteolytic, alcalase 0.6L and thermease for the oyster whereas MKC-acid fungal protease and thermoase for the mussel, respectively.

• Journal of Digital Convergence
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• v.14 no.1
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• pp.253-262
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• 2016

Yeonsan Ogae has been known as supporting health and high efficacy of treatment. In recent days, as the efficacy of functional peptides has known, the optimization of oligo peptides production and its characteristics from Ogae viscera has been performed. Response surface method was used to perform the optimizaion of enzyme hydrolysis. The range of processes was temperature (40, 50 and $60^{\circ}C$), pH(6.0, 7.0 and 8.0), and enzyme(1, 2 and 3%). The degree of hydrolysis, amono acids, molecular weight of products were analyzed. The optimum process of enzyme hydrolysis were determined as temperature $58^{\circ}C$, pH 7.5, and enzyme concetration 3%. At optimum conditions, the degree of hydrolysis after 2 h reaction was 75-80%. The total amino acids of amino acid and were 386.15 mg/100 g and 155.26 mg/100 g, respectively. The molecular weight of products by using Maldi-TOF was ranged from 300 to 1,000 Da.

• Korean Journal of Food Science and Technology
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• v.16 no.2
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• pp.228-234
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• 1984

A partial hydrolysis of soybean protein isolate was carried out by using pepsin and trypsin. The degree of hydrolysis was evaluated by chemical analysis, viscometric measurements and gel electrophoresis. The functional properties of the hydrolyzates such as flow behavior, emulsion properties and foaming properties were evaluated. A selective hydrolysis of 11S protein fraction by pepsin was observed from the SDS-PAG electrophoresis. The changes in the molecular weight distribution by different conditions of enzyme hydrolysis were evaluated. The changes in the intrinsic viscosity of the protein hydrolylate by reaction time were highly correlated to the contents of TCA soluble protein and 0.03 M $CaCl_2$ soluble nitrogen. The degree of hydrolysis ($DH_{TCA}$, $DH_{Ca}$) were used to evaluate the effect of enzyme treatment on the functional properties of the hydrolyzate. The apparent viscosity and emulsion capacity and stability of the protein solution decreased as DH increased, while the foaming capacity increased linearly with the increasing DH.

• Journal of Sericultural and Entomological Science
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• v.45 no.1
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• pp.46-57
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• 2003

This study was carried out to investigate the characteristics of the soluble sericins after degumming and after hydrolysis of insoluble sericin with various enzymes. Especially, the hydrolysis characteristics were examined in terms of molecular weight of the soluble sericin. Amino acid composition and molecular weight characteristics of the soluble sericins were also studied. When the insoluble sericin was hydrolyzed with kojizyme and flavourzyme, the solubility was highest at pH 7 and 50$^{\circ}C$. On the other hand, in the cases of protamex and alcalase, the highest solubility was obtained at 60$^{\circ}C$. In these cases, solubility increased with pH. In enzymatic hydrolysis, the solubility was increased with concentration of enzymes until 4 hours. After then, a slight difference was found along with treatment times. In enzymatic hydrolysis, the absorbance of the soluble sericin was increased with concentration of enzymes and treatment times. Average degree of polymerization was decreased with treatment time and concentration. The amino acid compositions were similar in low(low molecular weight by degumming) and high (high molecular weight by degumming). Those of PK (soluble sericin hydrolyzed with kojizyme), PP (soluble sericin hydrolyzed with protamex), and PA(soluble sericin hydrolyzed with alcalase) were similar to each other. Serine and tyrosine compositions were higher in low and high than those of PK, PP, and PA. However proline was absent in low and high. Molecular weights of the various sericins became higher as KP>high>PP>low>PA and those of KP and PA were 9,800 and 905 respectively.

• Asian-Australasian Journal of Animal Sciences
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• v.30 no.11
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• pp.1612-1619
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• 2017

Objective: The objective of this study was to optimize ultrasonic-assisted enzymatic hydrolysis conditions, including enzyme-to-substrate (E/S) ratio, pH, and temperature, for producing porcine liver hydrolysates (PLHs) with the highest 1,1-diphenyl-2-picrylhydrazyl (DPPH) free radical scavenging activity by using response surface methodology (RSM). Methods: The study used RSM to determine the combination of hydrolysis parameters that maximized the antioxidant activity of our PLHs. Temperature ($40^{\circ}C$, $54^{\circ}C$, and $68^{\circ}C$), pH (8.5, 9.5, and 10.5), and E/S ratio (0.1%, 2.1%, and 4.1%) were selected as the independent variables and analyzed according to the preliminary experiment results, whereas DPPH free radical scavenging activity was selected as the dependent variable. Results: Analysis of variance showed that E/S ratio, pH, and temperature significantly affected the hydrolysis process (p<0.01). The optimal conditions for producing PLHs with the highest scavenging activity were as follows: E/S ratio, 1.4% (v/w); temperature, $55.5^{\circ}C$; and initial pH, 10.15. Under these conditions, the degree of hydrolysis, DPPH free radical scavenging activity, ferrous ion chelating ability, and reducing power of PLHs were 24.12%, 79%, 98.18%, and 0.601 absorbance unit, respectively. The molecular weight of most PLHs produced under these optimal conditions was less than 5,400 Da and contained 45.7% hydrophobic amino acids. Conclusion: Ultrasonic-assisted enzymatic hydrolysis can be applied to obtain favorable antioxidant hydrolysates from porcine liver with potential applications in food products for preventing lipid oxidation.