• KSBB Journal
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• 제15권6호
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• pp.635-643
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• 2000

To compare the antioxidative activities of fish skin and bovine skin gelatin hydrolysate, gelatin hydrolysates from Alaska pollack and bovine skin were prepared by various enzymatic hydrolysis methods (1st step, Alcalase; 2nd step, pronase E; 3rd step, collagenase) using a continuous three-step membrane reactor. The molecular weight distributions of the 1st, 2nd and 3rd step hydrolysates were 7∼10 kDa, 2∼5 kDa and 0.7∼0.9 kDa, respectively. The antioxidative activity of fish skin gelatin hydrolysate was stronger than that of bovine skin gelatin hydrolysate, and in particular, both of 2nd step hydrolysates showed more antioxidative activity than hydrolysates of any other step. The optimum antioxidative activity concentration of the 2nd step hydeolysates of fish and boving skin were 1% (w/w) in a linoleic acid water-alcohol emulsion. In cultured cells exposed to t-butyl hydroperoxide (t-BHP), the 2nd step hydrolysate of fish skin gelatin delayed cell death most. These results suggest that the antioxidative activity of fish skin gelatin hydrolysate is higher than that of bovine skin gelatin hydrolysate because of their different amino acid contents.

• 한국수산과학회지
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• 제42권5호
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• pp.417-425
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• 2009

The potential utility of fish scales to the functional food industry has been investigated due to its antioxidant and antihypertensive characteristics. In this study, we report on the reactive oxygen species (ROS) scavenging and angiotensin I converting enzyme (ACE) inhibitory activities of gelatin hydrolysates processed from Branchiostegus japonicus scales, which are also high in protein content (about 46.1%). We prepared the enzymatic gelatin hydrolysates with four proteases (${\alpha}$-chymotrypsin, Alcalase, Neutrase and trypsin) from B. japonicus scale gelatin, which was prepared according to different reaction times, substrate/enzyme ratios and substrate concentrations. The enzymatic hydrolytic degrees of the gelatin increased time-dependently up to 6 hrs, while the Alcalase gelatin hydrolysates showed the highest hydrolysis degrees compared to the others. Furthermore, gelatin hydrolysates of Neutrase and ${\alpha}$-chymotrypsin showed the highest DPPH radical and $H_2O_2$ scavenging activities ($IC_{50}$ value; 9.18 mg/mL and 9.74 mg/mL), respectively. However, the activities were not significant (P<0.05). We also observed that the four gelatin hydrolysates significantly increased ACE inhibitory activities from approximately 20% to 60% (P<0.05), Among them, the Alcalase gelatin hydrolysates showed the higher ACE inhibitory activity ($IC_{50}$ value; 0.73 mg/mL) compared to the others. These results suggest that the enzymatic gelatin hydrolysates prepared from B. japonicus scales may possess a potentially useful function as an ACE inhibitory agent. As such, the utility of B. japonicus scales should be given due consideration for application in the functional food industry.

• Fisheries and Aquatic Sciences
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• 제12권2호
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• pp.79-85
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• 2009

Gelatin hydrolysates with a high inhibitory activity against angiotensin I-converting enzyme (ACE) were fractionated from Alaska pollock surimi refiner discharge. The ACE-inhibitory activity, expressed as $IC_{50}$ (mg/mL), was highest (0.49 mg/mL) in gelatin hydrolysates formed by sequential 2-hr treatments of Pronase and Flavourzyme. After fractionation through four different membrane filters with molecular weight cut-offs of 3, 5, 10, and 30 kDa, the highest ACE-inhibitory activity (0.21 mg/mL) was observed with the 3-kDa filtrate.

• Applied Biological Chemistry
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• 제37권2호
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• pp.85-93
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• 1994

연속식 2단계 막(MWCO 10,000, MWCO 5,000)반응기를 이용하여 어피젤라틴 가수분해물을 제조하여 그 가수분해물의 분자량, 아미노산조성 및 기능성에 대하여 검토하였다. 1단계 젤라틴 가수분해물의 분자량은 $8{\sim}10\;KDa$ 및 $4.5{\sim}6.5\;KDa$이 주종을 이루었으며, 2단계 가수분해물의 분자량은 $2{\sim}6\;KDa$ 및 2 KDa 이하의 저분자 펩타이드도 존재하였다. 어피젤라틴의 아미노산조성과 1단계 및 2단계 어피젤라틴 가수분해물의 아미노산조성 사이에는 거의 차이가 없었고, 감칠맛과 단맛에 관련이 있는 아미노산 함량이 전체의 $68{\sim}72%$에 달한 반면, 쓴맛을 내는 아미노산 함량은 $23{\sim}25%$에 불과하였으며, 1단계 가수분해물에 비해 2단계 가수분해물이 단맛과 감칠맛이 더 좋았다. 1단계 및 2단계 가수분해물의 용해도는 모든 pH영역에서 완전히 용해하였으나, 유화성 및 포말성은 거의 나타나지 않았다. 완충능은 2단계 가수분해물이 가장 높았으나, 점도는 모든 pH영역에서 거의 차이가 없었으며, 어피젤라틴 보다는 가수분해물의 점도가 더 낮았다. 그리고 2단계 가수분해물은 등온흡습도가 가장 높아 수분활성 저하제로서 이용할 수 있을 것으로 판단되었다.

• Preventive Nutrition and Food Science
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• 제4권1호
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• pp.14-17
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• 1999

Bovine hide and pig skin gelatins were prepared and their molecular weight profiles were examined by SDS-PAGE. The major molecular weights of bovine hide gelatin were 220 kDa, 140kDa, and 130kDa and the weights of pigskin gelatin were 210 kDa, 135kDa and 120kDa. Also , as a typical parameter of rheological property of the gelatin , viscosities of gelatin were measured under various conditions. Gelatin hydrolysates were prepared using typical commerical proteases and their angiotensin converting enzyme inhibitory activities were examined.

• 한국식품영양과학회지
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• 제39권4호
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• pp.587-594
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• 2010

다양한 기능적 특성을 가지는 단백질 가수분해물의 개발을 위하여, casein, ISP, wheat gluten, gelatin의 4종류 단백질 기질을 alcalase, bromelain, papain, neutrase, trypsin 등의 효소를 이용하여 가수분해물을 제조하였다. 각 단백질에 대한 효소 분해과정을 확인하기 위하여 pH-stat 방법을 이용하여 시간에 따른 단백질 가수분해도(DH)를 측정하였고, 단백질 종류와 효소 종류에 의한 쓴맛 정도와 단백질 가수분해물의 용해성을 검토하고자 DH 10%에서 가수분해를 종결짓고, pH 6.5에서 각각의 용해성과 쓴맛을 NSI(nitrogen soluble index) 측정과 관능검사로 비교하였다. 시간에 따른 가수분해도는 단백질에 따라 다양하게 나타났으며, Casein, ISP, wheat gluten, gelatin의 순으로 높게 나타났다. 모든 단백질에서 alcalase의 가수분해도가 가장 높았으며, neutrase, bromelain, papain의 가수분해도는 비슷한 정도를 보였다. 그러나 trypsin의 경우는 casein에서는 매우 높았지만, ISP에서는 가장 낮았다. DH 10%에서 casein은 trypsin 가수분해물이, ISP와 gluten은 brolmelain과 neutrase 가수분해물이, gelatin의 경우 사용된 모든 효소 가수분해물이 쓴맛이 약하고 용해도가 높아 좋은 기질-효소 조합으로 선택될 수 있었다. 따라서 쓴맛이 적고 용해도가 높은 단백질 가수분해물은 가수분해도의 조절과 단백질과 효소 조합의 선택, 단백질 가수분해물의 농도 조절 등으로 얻을 수 있었다.

• Fisheries and Aquatic Sciences
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• 제12권3호
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• pp.163-170
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• 2009

This study was conducted to obtain the gelatin fraction with a high anti oxidative activity from Alaska pollock surimi by-products using a two-step enzymatic hydrolysis and ultrafiltration. Among gelatin hydrolysates from refiner discharge of Alaska Pollock surimi, the highest antioxidative activity (81.5%) resulted from gelatin hydrolysate sequentially treated with Pronase E and Flavourzyme each for 2 hr. However, no difference was seen in the anti oxidative activity of the second hydrolysate (Pronase E-/Flavourzyme-treated hydrolysate) when compared to the permeate fractionated through a 10-kDa membrane. The results suggest that the Pronase E-/Flavourzyme-treated hydrolysate from refiner discharge gelatin of Alaska pollock surimi can be used as a supplementary raw material for improving health functionality.

• 한국수산과학회지
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• 제49권5호
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• pp.594-599
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• 2016

Infection with HIV (Human immunodeficiency virus), over time, develops into acquired immunodeficiency syndrome (AIDS). The development of non-toxic and effective anti-HIV drugs is one of the most promising strategies for the treatment of AIDS. In this study, we investigated the anti-HIV-1 activity of gelatin hydrolysates from Alaska pollack skin. Gelatin hydrolysates were prepared using four enzymes (alcalase, flavourzyme, neutrase, and pronase E). Among these, the pronase E gelatin hydrolysate was found to inhibit HIV-1 infection in the human T cell-line MT4. It exhibited inhibitory activity on HIV-1_IIIB-induced cell lysis, reverse transcriptase activity, and viral p24 production at noncytotoxic concentrations. Moreover, it decreased the activation of matrix metalloproteinase-2 (MMP-2) in vitro. Because HIV infection-induced activation of MMP-2 can accelerate collagen resolution and collapse of the immune system, pronase E gelatin hydrolysate might prevent the activation of MMP-2 in cells, resulting in collagen stabilization and immune cell homeostasis consistent with anti-HIV activation. These results suggest that pronase E gelatin hydrolysate could potentially be incorporated into a novel therapeutic agent for HIV/AIDS patients.

• 한국축산식품학회지
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• 제32권2호
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• pp.234-240
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• 2012

본 연구에서는 난소 제거로 인위적으로 골다공증이 유발된 흰쥐를 대상으로 돼지껍질에서 추출한 젤라틴과 저분자 젤라틴 효소분해물 급여가 골밀도에 미치는 영향을 조사하였다. 실험군의 구성은 10주령의 암컷 총 6군으로 난소 적출을 시행 하지 않은 일반 대조군과 난소 적출한 대조군은 일반식이를 급여하였으며, 난소 적출한 실험쥐에 3kDa 이하의 저분자 젤라틴 효소분해물을 0.1, 0.8% 첨가하고, 고분자 젤라틴을 0.1과 0.8% 첨가하여 급여한 후 그 효과를 비교하였다. 체중 증가량은 GH0.1, GH0.8 및 G0.8 급여구에서 NC와 OC에 비해 유의적으로 증가하였으며 특히 GH0.1과 GH0.8처리군은 사료섭취량이 NC와 OC에 비해 증가하였으나 사료효율은 유의적인 차이를 보이지 않았다. 대퇴골의 골밀도는 GH0.8처리군이 OC군에 비해 높았으나(p<0.05) NC의 수준에는 미치지 못하였다. 혈중 총 콜레스테롤 함량은 처리군간의 유의적인 차이를 보이지 않았으나 젤라틴 급여군과 GH 급여군의 HDL-C은 OC군에 비해 유의적인 증가를 나타내었다. 혈중 alkaline phosphatase(ALP)와 osteocalcin은 각각 GH0.1과 GH0.8에서 유의적인 감소를 나타내었다(p<0.05). 간질환의 지표인 혈중 GOT와 GPT도 모든 처리구에서 OC에 비해 유의적으로 감소하였다. 따라서 본 연구결과 돼지껍질에서 분리한 저분자 젤라틴 효소분해물은 골밀도를 증진시키고 폐경기 여성의 골건강에 도움을 줄 수 있는 수용성 기능성 소재로 이용 가능성이 있을 것으로 기대되지만 젤라틴 급여구의 높은 단백질 함량으로 젤라틴 효소분해물의 효과가 미미하여 비교시 골밀도 증진 효과의 유의적인 차이가 없어 추후 적정농도 설정에 관한 연구가 추가되어야 할 것으로 판단된다.

• Fisheries and Aquatic Sciences
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• 제14권1호
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• pp.1-10
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• 2011

This study was conducted to obtain hydrolysates with potent antioxidative activity from rockfish skin gelatin. Gelatin was extracted under high temperature/high pressure using a two-step enzymatic hydrolysis with commercial enzymes such as Alcalase, Flavourzyme, Neutrase, and Protamex. The second rockfish-skin gelatin hydrolysate (SRSGH) was prepared by further incubating the first gelatin hydrolysate (FRSGH), which had been hydrolyzed with Alcalase for 1-h (FRSGH-A1), with Flavourzyme for 2-h (SRSGH-F2). The second gelatin hydrolysate showed higher antioxidative activity of 3.72 as measured by a Metrohm Rancimat and superior angiotensin I-converting enzyme (ACE) inhibiting activity of 0.82 mg/mL. Compared with the gelatin, the relative proportion in SRSGH-F2 was markedly decreased in the 100-kDa peak, whereas it was increased in that less than 100-kDa. The amino acid composition of SRSGH-F2 was rich in glycine (25.9%), proline (10.8%), alanine (9.1%), and glutamic acid (9.1%). In contrast, it was poor in cystine (not detected), methionine (1.6%), tyrosine (0.4%), hydroxylysine (0.9%), and histidine (0.9%). In recent years, demand for natural functional foods has been increasing, and SRSGH-F2 can be used as a functional food ingredient in the food industries. However, further detailed studies on SRSGH-F2 with regard to its antioxidant activity in vivo and the various antioxidant mechanisms are needed.