Optimization of Enzymatic Production of Oligopeptides from Apricot Almonds Meal with Neutrase and N120P

被引:8
作者
Wang, Chunyan [1 ]
Wang, Qiang [1 ]
Tian, Jinqiang [1 ]
机构
[1] Chinese Acad Agr Sci, Inst Agrofood Sci & Technol, Key Lab Agrofood Proc & Qual Control, Minist Agr, Beijing 100193, Peoples R China
关键词
apricot almonds meal; enzymatic production; hydrolysis; oligopeptides; INHIBITORY PEPTIDES; PROTEIN; ACID;
D O I
10.3390/ijms11124952
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Neutrase 0.8L and N120P proteases were used for oligopeptide production from apricot almonds meal, and response surface design was carried out to optimize the effect of hydrolysis conditions on hydrolysis degree (DH) and oligopeptide yield rate. Four independent variables were used to optimize the hydrolysis process: hydrolysis temperature (X-1), enzyme-to substrate ratio (E/S) (X-2), substrate concentration (X-3) and reaction time (X-4). Statistical analysis indicated that the four variables, quadratic terms of X-1, X-3, and X-4, and the interaction terms with X-1 had a significant (p < 0.05) effect on DH. The yield rate was also significantly affected by the four variables and quadratic terms of X-1, X-2 and X-4. Two mathematical models with high determination coefficient were obtained and could be employed to optimize protein hydrolysis. The optimal hydrolysis conditions were determined as follows: hydrolysis temperature 52.5 degrees C; enzyme-to-substrate ratio (E/S) 7200 U/g; substrate concentration 2%; reaction time 173 min. The initial pH 6.5 and Neutrase-to-N120P dosage ratio 2: 1 were fixed in this study according to the preliminary research. Under these conditions, the experimental DH and yield rate were 34.10 +/- 5.25% and 72.42 +/- 2.27%, respectively.
引用
收藏
页码:4952 / 4961
页数:10
相关论文
共 25 条
[1]   Almond (Prunus dulcis L.) protein quality [J].
Ahrens, S ;
Venkatachalam, M ;
Mistry, AM ;
Lapsley, K ;
Sathe, SK .
PLANT FOODS FOR HUMAN NUTRITION, 2005, 60 (03) :123-128
[2]   Kernel fatty acid and triacylglycerol composition for three almond cultivars during maturation [J].
Cherif, A ;
Sebei, K ;
Boukhchina, S ;
Kallel, H ;
Belkacemi, K ;
Arul, J .
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 2004, 81 (10) :901-905
[3]   INVITRO DIGESTIBILITY, PHYSICOCHEMICAL AND FUNCTIONAL-PROPERTIES OF APRICOT KERNEL PROTEINS [J].
ELAAL, MHA ;
HAMZA, MA ;
RAHMA, EH .
FOOD CHEMISTRY, 1986, 19 (03) :197-211
[4]   WHEY-PROTEIN ANTIGENICITY REDUCTION BY FUNGAL PROTEINASES AND A PEPSIN PANCREATIN COMBINATION [J].
ENA, JM ;
VANBERESTEIJN, ECH ;
ROBBEN, AJPM ;
SCHMIDT, DG .
JOURNAL OF FOOD SCIENCE, 1995, 60 (01) :104-&
[5]  
Gauthier S.F., 2006, INT DAIRY J, V16, P197
[6]  
Gezer I, 2003, J FOOD ENG, V56, P49, DOI 10.1016/S0260-8774(02)00147-4
[7]   ENZYMATIC-HYDROLYSIS OF WHEY PROTEINS .1. KINETIC-MODELS [J].
GONZALEZTELLO, P ;
CAMACHO, F ;
JURADO, E ;
PAEZ, MP ;
GUADIX, EM .
BIOTECHNOLOGY AND BIOENGINEERING, 1994, 44 (04) :523-528
[8]   Purification and identification of angiotensin converting enzyme inhibitory peptides from beef hydrolysates [J].
Jang, A ;
Lee, M .
MEAT SCIENCE, 2005, 69 (04) :653-661
[9]   Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase [J].
Kuba, M ;
Tana, C ;
Tawata, S ;
Yasuda, M .
PROCESS BIOCHEMISTRY, 2005, 40 (06) :2191-2196
[10]   Antibacterial activity of peptides and folding variants from milk proteins [J].
Lopez Exposito, Ivan ;
Recio, Isidra .
INTERNATIONAL DAIRY JOURNAL, 2006, 16 (11) :1294-1305