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사과 추출물의 구취억제효과에 대한 Polyphenol Oxidase의 영향
조상원(Sang-Won Cho),곽기석(Ki-Suk Kwak),이주항(Joo-Hang Lee),윤영수(Young-Soo Yun),구연숙(Yeun-Suk Gu),지청일(Cheong-Il Ji),이두석(Doo-Seog Lee),이양봉(Yang-Bong Lee),김선봉(Seon-Bong Kim) 한국식품영양과학회 2001 한국식품영양과학회지 Vol.30 No.6
본 연구는 사과의 구취억제인자를 구명하기 위한 기초자료로써 사과 추출물의 획분에 따른 사과에서 추출한 PPO의 methyl mercaptan에 대한 구취억제활성을 조사하였다. 사과를 착즙하여 구취억제활성을 측정해 본 결과, 사과 고형분의 농도가 증가함에 따라 구취억제활성이 증가하는 경향을 나타내었다. 사과의 저분자획분에 PPO를 첨가한 경우, 저분자획분의 농도증가 및 반응시간에 따른 methyl mercaptan에 대한 구취억제활성이 증가하는 경향을 나타내었다. 이상의 결과는 사과에서 추출한 PPO에 의한 갈변반응의 중간체로 생성되는 o-quinone이 methyl mercaptan과 결합하여 methyl mercaptan을 비휘발성으로 전환시켜 구취억제활성을 나타내는 것으로 생각된다. Deodorizing activity of polyphenol oxidase (PPO) extracted from apples was investigated by measuring the changes of methyl mercaptan as an indicator of halitosis in human mouths. In the studies of apple extracts on deodorizing activity, the deodorizing activity was increased with the amount of apple extracts. In the cases of adding PPO to the low molecular fraction of apple extracts, the deodorizing activities were increased with the amount of the low molecular fraction of apple extracts and the reaction time of the extracts with PPO. Deodorizing activities of PPO is thought that o-quinone as an intermidiate produced by an oxidative reaction of PPO during enzymatic browning reactions may react with methyl mercaptan to form a non-volatile and sulfur-containing compound.
단백질 분해효소를 이용하여 제조한 속성 멸치 액젓의 팹티드 특성 1. 단백질 분해효소에 의한 멸치 액젓 및 Actomyosin 의 가수분해
김인수(In Soo Kim),최영준(Yeung Joon Choi),허민수(Min Soo Heu),조영제(Toung Je Cho),임영선(Yeong Sun Im),구연숙(Yeun Suk Gu),여생규(Saeng Gyu Yeo),박재윤(Jae Woon Park) 한국수산과학회 1999 한국수산과학회지 Vol.32 No.4
The optimal conditions of enzymatic hydrolysis for preparation of rapid salted and fermented anchovy sauce (SFAS) using various proteases such as trypsin, chymotrypsin, crude enzyme from squid liver and viscera, Alcalase, Neutrase and Protamex were studied. SFAS prepared with squid viscera had higher level of VBN (173.6 ㎎/100 g) when stored for 70 days than other samples, and peroxide values were almost equal among all samples during fermentation period. Total amino acids and nonprotein nitrogenous compounds remarkably increased as SFAS treated with Alcalase or Protamex which exhibited higher the hydrolysis rate of 57% at 60 day than others. The optimal pHs of trypsin, chymotryosin, Alcalase, Neutrase and Protamex on anchovy actomyosin were 7.5, 6.5, 6.5, 7.0 and 5.0, respectively. Optimal temperatures of trypsin, chymotryosin, Alcalase and Neutrase were 55, 45, 60 and 55℃, respectively. Otherwise, Protamex activity increased as temperature increased from 20 to 70℃. Protamex had higher K_m (3.545) and K_(max) value (2.688) than others. Protamex affected less by NaCl had 52.5% activity at the fermentation conditon of 20℃ and 25% NaCl. Protamex appeared to be very effective for the hydrolysis of crude actomyosin from anchovy.
멸치육 효소 가수분해물의 Angiotensin 전환효소 저해작용
이태기(Tae Gee Lee),박영범(Yeung Beom Park),박덕천(Douck Chon Park),염동민(Dong Min Yeum),김인수(In Soo Kim),구연숙(Yeun Suk Gu),박영호(Yeung Ho Park),김선봉(Seon Bong Kim) 한국수산과학회 1998 한국수산과학회지 Vol.31 No.6
To develop functional food material with angiotensin converting enzyme (ACE) inhibitory peptides, muscle protein of anchovy, Engraulis japonica was hydrolyzed during 48 hrs by digestive proteases such as pepsin, trypsin, α-chymotrypsin, and commercial proteases such as papain, bromelain, complex enzyme, Flavourzyme, Novozym, Neutrase, Protamex and Alcalase. The only 50% ethanol soluble hydrolysates were tested for inhibitory activity against ACE and yield of 50% ethanol soluble peptide-nitrogen (ESPN_(50)). ACE inhibition effects and yield of ESPN_(50) occurred as hydrolysis time increased to 8 hrs. Among those proteases tested, hydrolysates by Alcalase and α-chymotrypsin had greater ACE inhibitory activity (80 and 74%, respectively) with elevated levels of ESPN_(50) (48 and 58 ㎎/㎖, respectively), while Protamex hydrolysates had greater ACE inhibitory activities (73%) with reduced levels of ESPN_(50) (7.2 ㎎/㎖) than others. Amino acid compositions of 50% ethanol solubles obtained from those hydrolysates were rich in glutamic acid, aspartic acid, cysteine and leucine.