• 한국약용작물학회지
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• 제19권2호
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• pp.77-82
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• 2011

The antioxidative activity of various enzymatic extracts from Sarcodon aspratus (S. aspratus) was evaluated by measuring 1,1-diphenyl-2-picrylhydrazyl (DPPH), and alkyl radical scavenging activity using an electron spin resonance (ESR) spectrometer. For this study, the S. aspratus were enzymatically hydrolyzed by seven carbohydrases (Viscozyme, Celluclast, Dextrozyme, AMG, Promozyme, Maltogenase, and Termamyl) and eight proteases (${\alpha}$-chymotrypsin, Alcalase, Flavourzyme, Neutrase, papain, pepsin, Protamax, and trypsin). The DPPH radical scavenging activities of Viscozyme and pepsin extracts were the highest, and the half maximal inhibitory concentration ($IC_{50}$) values were 0.896 and 0.734mg/mL, respectively. The Celluclast and trypsin extracts showed the highest scavenging activities on alkyl radical, and their $IC_{50}$ values were 0.278 and 0.575mg/mL, respectively. The Celluclast extracts was decreased cell apoptosis in PC-12 cells against $H_2O_2$-induced oxidative damage. The findings of the present study suggest that enzymatic extracts of S. aspratus exhibit antioxidative activity against oxidative stress on PC-12 cells.

• 한국수산과학회지
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• 제39권3호
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• pp.269-277
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• 2006

This study prepared functional oyster hydrolysates using two-step enzymatic hydrolysis and investigated their functional properties. To prepare two-step enzymatic hydrolysates (TSEH), oysters were hydrolyzed using 1% Protamex (PR) at $40^{\circ}C$ and pH 6.0 for 1 hr before sequential treatment with one of the following enzymes for 1 hr: Alcalase (AL), Flavourzyme (FL), Neutrase (NE), pepsin (PE), and trypsin (TR). The PRAL, PRNE and PRTR hydrolysates had significantly greater angiotensin I converting enzyme (ACE) inhibitory activity than did PR and the other TSEHs. Only the antioxidant activity of the PRNE hydrolysate was significantly different (p<0.05), while none of the TSEHs had antimicrobial activity. The oyster hydrolysate prepared by sequential treatment with Protamex and Neutrase (PRNE) had the best ACE inhibitory activity and antioxidant activity, with $IC_{50}$ values of 0.40 and 0.94 mg/mL, respectively. The PRNE hydrolysate was processed through an ultrafiltration (UF) series with molecular weight cut-off (MWCO) membranes of 3, 5, 10, and 30 kDa, and the ACE inhibitory, antioxidant, and antimicrobial activities of the permeates were determined. The permeate through the 3-kDa MWCO membrane had greater ACE inhibitory activity and antioxidant activity than did the other PRNE permeates, with $IC_{50}$ values of 0.11 and 0.40 mg/mL, respectively.

• 한국축산식품학회지
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• 제22권1호
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• pp.87-93
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• 2002

최근 고혈압을 예방하기 위한ACE 저해 펩타이드에 대한 연구는 주로 여러 가지 식품 단백질의 효소 가수분해물로부터 얻어진 펩타이드를 중심으로 이루어지고 있다. 본 연구에서는 케이신을 여러 가지 상업용 단백질분해 효소를 사용하여 ACE저해 효과가 높은 가수분해물 제조시 가수분해 조건이 ACE저해효과에 미치는 영향을 알아보자 하였으며 적정 가수분해 조건을 설정하고자 하였다. ACE 저해효과를 가지는 케이신 가수분해 물을 제조하기 위한 효소 종류, 첨가량 및 가수분해시간은 효소는 Aspergillus oryzae 유래의 promod 192를 사용하고, 효소의 첨가량은 케이신에 대하여 1%, 반응시간은 47$^{\circ}C$에서 12시간으로 하는 것이 적당하였다. 이 때 케이신 가수분해물의 $IC_{50}$/값은 248.71ug/m1(통상법), 265.84ug/ml(전처리법)로서 ACE 저해효과가 높았다.

• 한국식품과학회지
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• 제31권2호
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• pp.391-398
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• 1999

국내산 생강의 높은 원료비를 극복하면서 품질이 우수한 중간소재성 가공제품을 개발하기 위하여 효소적 추출기법을 적용하였을 때의 수율 및 품질변화를 조사하였다. 생강을 1차 착즙하고 남은 잔사를 $\alpha$-amylase로 가수분해한 후 2차 착즙하고 다시 남은 잔사에 90% 에탄올로 $30^{\circ}C$에서 1시간 추출하여 각각 착즙액을 혼합할 경우 단순 착즙액보다 동일 $^{\circ}Brix$ 기준으로 약 2.8배 정도, 펄프보다는 건물기준으로 약 5배 이상 착즙수율을 증진시킬 수 있었다. 이와 같이 제조된 최종 추출액에는 착즙액 보다 조섬유가 약 62%, 전분이 48%정도 감소하는 결과를 나타내어 작업공정의 개선이 가능함을 알 수 있었다. 또한 최종 추출액은 착즙액에 비하여 유리아미노산이 약 40% 정도 소실한 반면 유리당은 약 270% 증가하는 결과를 보여주고 있어, 생강의 효소적 추출법은 생강 가공제품 제조시 단맛을 강화하는 효과를 제공할 수 있었다.

• 한국식품과학회지
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• 제40권3호
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• pp.290-296
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• 2008

찹쌀 전분을 가교화 후 4가지 상업용 ${\alpha}$-amylase 효소와 반응시켜 CLE 찹쌀 전분을 제조하고 이들의 이화학적 특성을 연구하였다. CLE 찹쌀 전분의 팽윤력 및 용해도는 천연 찹쌀 전분에 비해 다소 증가되는 경향을 보였다. 등온흡습곡선에서는 CLE 처리에 따른 수분 감소현상을 보였으나 유의적인 차이는 없었다. RVA특성을 검토한 결과 Termamyl과 Liquozyme으로 처리한 찹쌀 전분은 전반적으로 효소에 의한 가수분해가 강하게 진행되어 온도에 따른 점도의 변화가 크게 나타나지 않았으며, Fungamyl과 Kleistase로 처리한 찹쌀 전분은 효소에 의한 가수분해가 상대적으로 미약하게 진행되어 가교화에 의한 특성을 더 많이 나타내었다. DSC 열적 특성의 경우 호화개시온도, 호화종결온도 그리고 호화온도범위, 호화 엔탈피 모두 각 전분간에 유의적인 차이가 나타나지 않았다. X-ray 회절 분석 결과 또한 CLE 찹쌀 전분과 천연 찹쌀 전분 모두 A형의 결정 형태를 나타내었고, 상대적 결정화도의 차이가 나타나지 않는 것으로 보아 가교화 및 가교화후 효소처리가 찹쌀 전분의 결정형영역에는 영향을 주지 않는 것으로 보여진다.

• Journal of Ginseng Research
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• 제23권1호
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• pp.50-54
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• 1999

In this paper, the saponin enzymatic hydrolysis of ginsenoside Rg3 was studied. The $ginsenoside-{\beta}-glucosidase$ from FFCDL-48 strain mainly hydrolyzed the ginsenoside Rg3 to Rh2, the enzyme from FFCDL-00 strain hydrolyzed Rg3 to the mixture of Rh2 and protopanaxadiol (aglycon). The $ginsenoside-{\beta}-glucosidase$ from FFCDL-48 strain was purified with a column of DEAE-Cellulose to one spot in the SDS polyacrylamide gel electrophoresis. During the purification, the enzyme specific acitvity was increased about 10 times. The purified $ginsenoside-{\beta}-glucosidase$ can hydrolyze the Rg3 to Rh2, but do not hydrolyze the $p-nitrophenyl-{\beta}-glucoside$ which is a substrate of original exocellulase such as ${\beta}-glucosidase$ of cellulose. The molecular weight of $ginsenoside-{\beta}-glucosidase$ was 34,000, the optimal temperature of enzyme reaction was $50^{\circ}C,$ and the optimal pH was 5.0.

• Journal of Microbiology and Biotechnology
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• 제9권4호
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• pp.509-513
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• 1999

The molecular size reduction and the formation of bitterness during a tryptic hydrolysis of soybean 11S glycinin were determined by using quantitative analysis and organoleptic evaluation. The 11S glycinin of 90% purity was prepared by cryoprecipitation and Con A Sepharose 4B affinity chromatography, and hydrolyzed with trypsin in a pH-stat reactor for 4 h. Bitterness was formed within 1 h of hydrolysis, and then slowly increased up to $3.5\times10^{-5}$ M quinine-HCl equivalent. The extent of hydrolysis (DH) was 7% at 1 h and increased up to 12% by the end of the reaction. The -amino nitrogen content increased from an initial 0.7 mM to 7 mM at the end of the period. The SDS-PAGE analysis showed that the acidic subunit of 11S glycinin was mostly hydrolyzed. The GP-HPLC analysis indicated that the bitterness was mainly contributed by the peptide fractions of molecular weights of 360-2,100 Da.

• Journal of Microbiology and Biotechnology
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• 제16권7호
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• pp.1047-1052
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• 2006

A bile salt hydrolase (BSH) was purified from Lactobacillus plantarum CK 102 and its enzymatic properties were characterized. This enzyme was successfully purified using ion-exchange chromatography with Q-Excellose and hydrophobic interaction chromatography with Butyl-Excellose. The purified enzyme showed a single protein band of 37 kDa by SDS-polyacrylamide gel electrophoresis, which was similar to the molecular weight of known BSHs. The amino acid sequence of GLGLPGDLSSMSR, determined by MALDI-TOF, was identical to that of BSH of L. plantarum WCFS1. Although this BSH hydrolyzed all of the six major human bile salts, glycine-conjugated bile acid was the best substrate, based on its specificity and $K_{m}$ value. Among the various substrates, the purified enzyme maximally hydrolyzed glycocholate with apparent $K_{m}$ and $V_{max}$ values of 0.5 mM and 94 nmol/min/mg, respectively. The optimal pH of the enzyme ranged from 5.8 to 6.3. This enzyme was strongly inhibited by thiol enzyme inhibitors such as iodoacetate and periodic acid.

• Journal of Microbiology and Biotechnology
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• 제14권3호
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• pp.607-611
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• 2004

Glycinin, one of the predominant storage proteins in soybeans, was examined as to whether it could be used as a calcium-binding mediator after chemical phosphorylation and enzymatic hydrolysis. Glycinin is composed of six subunits. One of the proglycinin subunits $(A_{la}B_{lb})$ was overexpressed in E. coli to obtain nonphosphorylated proteins with homogeneity. To investigate the enhanced calcium-binding properties of the phosphopeptides, the proglycinin was purified, phosphorylated, and hydrolyzed with trypsin. The proglycinin expressed in E. coli was purified by ammonium sulfate precipitation, ion-exchange chromatography, and cryoprecipitation. Chemical phosphorylation by sodium trimetaphosphate was performed to obtain phosphorylated proglycinin. After the phosphorylation, one-dimensional isoelectric focusing gel electroanalysis confirmed the phosphorylation of the proglycinin. The phosphorylated peptides were then hydrolyzed with trypsin, followed by a binding reaction with calcium chloride. The calcium-bound phosphopeptides were finally separated using immobilized metal $(Ca^{2+})$ chromatography. Consequently, a limited tryptic hydrolysate of the isolated phosphopeptides exhibited an enhanced calcium-binding ability, suggesting the potential of glycinin phosphopeptides as a calcium-binding mediator with greater availability.

• 한국미생물·생명공학회지
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• 제40권4호
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• pp.356-363
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• 2012

The aim of this study was to utilize rice bran, the main waste product of paddy processing, in xanthan gum production by Xanthomonas campestris fermentation. Deffated rice bran was enzymatically hydrolyzed using cellulase, gluco-amylase, alpha-amylase and xylanase at various pHs and temperatures within 0-12 h. The highest sugar content reached at $35^{\circ}C$, pH 5.5 in 6 h with 41.66%. The enzymatic hydrolysate was used as the carbon source for xanthan gum production by X. campestris NRRL B-1459 and X. campestris pv. campestris. The highest productivities obtained were 21.87 and 17.10 g/L, respectively. Viscosity measurement for the obtained xanthan gums and commercial gum was carried out in gum solutions at various pHs and temperatures. The highest viscosity was reached with 1% gum solutions at $20^{\circ}C$ and pH 5.5 for all gums with viscosity values of 470, 131 and 138 mPa sec, respectively. This work has provided relevant scientific information about the use of rice bran, an abundant agroindustrial residue, to produce xanthan gum.