• Fisheries and Aquatic Sciences
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• 제24권12호
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• pp.406-414
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• 2021

The objective of this study was to investigate the yield and characteristics of collagen protein extracted from the muscle of four different species of mantis shrimp: Miyakella nepa, Harpiosquilla harpax, Erugosquilla woodmasoni, and Odontodactylus cultrifer. Mantis shrimp muscle was extracted by using a pepsin-solubilization technique, with 0.5 M acetic acid and 5% pepsin enzyme. The highest collagen yield was from M. nepa muscle (0.478 ± 0.06%), which was significantly greater (p < 0.05) than that from H. harpax, O. cultrifer, and E. woodmasoni (0.313 ± 0.03%, 0.123 ± 0.02%, and 0.015 ± 0.00%, respectively). The freeze-dried collagen appeared as thin fibers, and formed an opaque film. The pepsin-soluble collagen (PSC) from four mantis shrimp species was analyzed by gel electrophoresis. The results showed that all species of mantis shrimp contained type I collagen, consisting of β, α1, and α2 subunits with average molecular weights of 250, 145, and 118 kDa, respectively. The study of the solubility of collagen showed that, for NaCl, collagen had the highest relative solubility in 2% NaCl (80.20 ± 4.95%). In contrast, the solubility decreased at higher NaCl concentrations. However, in terms of pH, collagen had the highest relative solubility at pH 3 (91.32 ± 5.14%), and its solubility decreased at higher pH. FT-IR spectroscopy was used to compare the collagen with a model compound. Five wavenumbers in the spectrum for model collagen were identified: Amide A (3,406-3,421 cm^-1), amide B (2,916-2,940 cm^-1), amide I (1,639-1,640 cm^-1), amide II (1,539-1,570 cm^-1), and amide III (1,234-1,250 cm^-1).

• 한국축산식품학회지
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• 제38권1호
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• pp.143-151
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• 2018

The effects of proteolytic enzymes (bromelain and bromelain+papain) and a ginger extract were assessed on collagen content and solubility, thermal shrinkage temperature of connective tissue, pH, cooking loss, drip loss, and Warner-Bratzler shear force (WBSF) of M. pectoralis profundus isolated from the beef brisket cut. Both proteolytic enzymes and ginger extract led to a significant increase in cooking loss and collagen solubility compared with untreated controls. On the other hand, the peak ($T_p$) thermal shrinkage temperature markedly decreased in all treatments compared with those in controls. Samples treated with bromelain, bromelain + papain, and ginger extract showed a significant decrease in WBSF by 36%, 40%, and 37%, respectively, compared with untreated controls. Our findings suggest that ginger extract are useful for post-mortem tenderization of meat containing high levels of collagen, compared to control even though, bromelain and bromelain + papain treatments have higher collagen solubility than ginger extract.

• 한국수산과학회지
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• 제42권6호
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• pp.574-579
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• 2009

Acid- and pepsin-solubilized collagens were extracted from the skin of shark (Isurus oxyrinchus) and their physicochemical properties were characterized by amino acid analysis, SDS-PAGE, the composition of collagen types, solubility and denaturation temperature. Acid - and pepsin-solubilized collagens from shark skin had an imino acid of 188.8 and 186.2 residues/1,000 amino acids, respectively. SDS-PAGE showed two different${\alpha}$ chains ($\alpha1$ and $\alpha2$) and $\beta$-component. The component ratio of type I and V was 10:1, and the type III was not found. Solubility of acid-soluble collagen was low in the range of pH 6.0 to pH 11.0. On the other hand, pepsin-solubilized collagen showed a low solubility in the range of pH 7.0-9.0. Temperature for denaturation of acid- and pepsin-solubilized collagens were $25^{\circ}C$ and $27^{\circ}C$, respectively.

• 한국축산식품학회지
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• 제43권3호
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• pp.491-501
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• 2023

Comparing the effects of sodium tripolyphosphate (STPP) concentrations of 0.2% and 0.4% on beef semitendinosus is the objective of the current investigation. The samples were cooked at varied temperatures (45+60℃ and 45+70℃) and times (1.5+1.5 h and 3+3 h) using staged cooking. The colour properties, cooking loss, water retention, shear force, water-holding capacity, sarcoplasmic, and myofibrillar solubility, and total collagen were investigated. The cooking time and temperature affected the water-holding capacity, cooking loss, CIE L^*, CIE a^*, CIE b^*, myofibrillar, and sarcoplasmic solubility, with lower temperature and short time having the lower detrimental effect. However, the significant effect can be intensified after the addition of STPP with higher water-holding capacity and tender meat obtained with 0.4% phosphate concentration at any cooking conditions. The STPP lowered the collagen content and increased the protein solubility of myofibrillar and sarcoplasmic, which this degradation is used as a good indicator of tenderness.

• Food Science and Biotechnology
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• 제17권1호
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• pp.26-30
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• 2008

This study was conducted to identify the effect of chilling temperature (-3 and $6^{\circ}C$) and aging (1- and 7-day) on objective meat quality, collagen solubility, and free amino acids in pork (longissimus muscle of Yorkshire). Warner-Bratzler (WB)-shear force indicated that variation in chilling temperature had no detectable effect on meat tenderness and tenderization during the 7-day aging period. Among the 13 detected free amino acids, only 3 amino acids (histidine, valine, leucine) were significantly affected by the temperature treatment (p<0.05). Collagen solubility was significantly increased at $6^{\circ}C$ treatment (p<0.05). There was a significant linear relationship (r=0.67, p<0.05) between changes in free amino acids and WB-shear force during the 7-day aging period. These results confirmed that chilling conditions had significantly affected collagen solubility, and meat tenderization occurred in direct proportion to an increase in free amino acids.

• 한국축산식품학회:학술대회논문집
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• 한국축산식품학회 2006년도 정기총회 및 제37차 춘계 국제학술발표대회
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• pp.94-97
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• 2006

Proteolytic enzymes and ginger extract were effective on tenderising M. pectoralis profundus, resulting in higher collagen solubility, a decrease of melting denaturation temperature and WBSF compared with the control. Comparing all treatments, bromelain treatment showed to be higher for collagen solubility than other treatments, but no significant differences in onset and melting denaturation temperature of intramuscular connective tissue were found. These corresponded to WBSF results. The present study indicates that ginger extract might be effectively able to be utilised in pilot level as better alternatives to bromelain and papain for tenderisation of tough meat, such as cull cow and beef cuts with many collagen.

• 한국축산식품학회지
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• 제33권4호
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• pp.474-480
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• 2013

This study was performed to investigate the effects of high pressure/high temperature (HPHT) treatment on the recovery efficiency and characteristics of porcine placenta hydrolysates. The placenta hydrolysates were characterized by solubility, free amino acid contents, gel electrophoresis, gel permeation chromatography (GPC) and amino acid composition. Placenta was treated at 37.5 MPa of pressure combined with various temperatures (150, 170, and $200^{\circ}C$) or various holding times (0, 30, and 60 min at $170^{\circ}C$). Insoluble raw placenta collagen was partially solubilized (> 60% solubility) by the HPHT treatment. Free amino group content of placenta collagen was increased from 0.1 mM/g collagen to > 0.3 mM/g collagen after HPHT treatment, reflecting partial hydrolysis of collagen. The molecular weight ($M_w$) distribution showed evidence of collagen hydrolysis by shifting of $M_w$ peaks toward low molecular weight when treated temperature or holding time was increased. Alanine (Ala), glycine (Gly), hydroxyproline (Hyp), and proline (Pro) contents increased after the HPHT treatments compared to a decrease in the others. In particular, the increase in Gly was obvious, followed by Hyp and Pro, reflecting that placenta hydrolysates were mainly composed of these amino acids. However, increasing temperature or holding time hardly affected the amino acid compositions. These results indicate that the HPHT treatment is advantageous to hydrolyze collagen derived from animal by-products.

• Asian-Australasian Journal of Animal Sciences
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• 제4권4호
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• pp.407-410
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• 1991

The relationship between the possible structural change due to chemical modifications and functionality changes was studied in pigskin collagen. Amino groups in collagen were modified by succinylation and reductive alkylation. Carboxyl groups were modified using carbodiimide. Thermal denaturation temperature of collagen increased remarkably by carboxyl groups modification whereas decreased by succinylation and reductive alkylation. Emulsifying capacity was improved by reductive alkylation and carboxyl groups modification while emulsion stability was improved by succinylation. Chemical modifications increased solubility whereas decreased the foaming capacity of collagen. Viscosity of collagen at various pH varied with methods of modification.

• Fisheries and Aquatic Sciences
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• 제13권2호
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• pp.102-111
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• 2010

This study was conducted to investigate the optimal conditions of collagen extraction from scales of yellowfin tuna (Thunnus albacares) using surface response methodology. Four independent variables of NaOH concentration and pretreatment fime in alkali pretreatment and enzyme concentration and treatment time in enzyme hydrolysis were used to predict a model equation for the collagen yield. The determinant coefficient ($R^2$) for the equation was 0.906. The values of the independent variables for the maximum yield were 0.32 N NaOH, 16.38 h alkali pretreatment time, 0.18% enzyme concentration, and 31.02 h enzyme treatment time. In the physicochemical properties of tuna scale collagen, sodium dodecyl sulfate-polyacrylamide gel electrophoresis of tuna scale collagen showed the same migration distances as that of calf skin collagen. The amide A, I, II, and III regions of tuna scale collagen in Fourier transform infrared measurements were shown in the peaks of 3,414 $cm^{-1}$, 1,645 $cm^{-1}$, 1,553 $cm^{-1}$, and 1,247 $cm^{-1}$, respectively. The amount of imino acids in tuna scale collagen was 18.97% and the collagen denaturation temperature was $33^{\circ}C$. The collagen solubility as a function of NaCl concentration decreased to 4% NaCl (w/v) and the collagen solubility as a function of pH was high at pH 2-4 and sharply decreased from pH 4 to pH 7. Viscosity of the collagen solution decreased continuously until $30^{\circ}C$ and this decreasing rate slowed in the temperature range of $35-50^{\circ}C$.

• 한국재료학회:학술대회논문집
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• 한국재료학회 2011년도 춘계학술발표대회
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• pp.54.2-54.2
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• 2011

DTBP (dimethyl 3,3`-dithiobispropionimidate) was applied to collagen and gelatin coating on BCP granules and a crosslinking agent. The DTBP crosslinking was done for decreasing the solubility of the coating and hence increasing the stability. The nanostructure of collagen and gelatin coating surfaces were observed by SEM technique. Based on the DSC thermograms and FT-IR spectrums, the crosslinkings were confirmed between collagen molecules and gelatin molecules. The compressive strength was measured before crosslinking and after that. In-vitro study was carried out by measuring cell viability and observing cell morphology after DTBP crosslinking. Moreover, the proliferation ability of MG-63 osteoblast-like cells on the crosslinked BCP granules was evaluated by Western blot assay. The BCP granules were implanted into rabbit femur for 4 weeks and 12 weeks. The bone tissue formation was analyzed with micro-computed tomography (micro-CT) and histological analysis was also carried out by hematoxylin and eosin (H&E) staining for visualization of cells.