scholarly journals Characterization of Goat Milk Hydrolyzed by Cell Envelope Proteinases from Lactobacillus plantarum LP69: Proteolytic System Optimization, Bioactivity, and Storage Stability Evaluation

Molecules ◽  
2018 ◽  
Vol 23 (6) ◽  
pp. 1317 ◽  
Author(s):  
Guowei Shu ◽  
Jie Huang ◽  
Li Chen ◽  
Ni Lei ◽  
He Chen
2019 ◽  
Vol 9 ◽  
Author(s):  
Tong Dan ◽  
Haiyan Chen ◽  
Ting Li ◽  
Jiale Tian ◽  
Weiyi Ren ◽  
...  

2017 ◽  
Vol 51 (6) ◽  
pp. 463-469 ◽  
Author(s):  
Wanticha Savedboworn ◽  
Sureeporn Niyomrat ◽  
Janyawan Naknovn ◽  
Kriangkrai Phattayakorn

Nutrients ◽  
2018 ◽  
Vol 10 (5) ◽  
pp. 633 ◽  
Author(s):  
Miriam Moreno-Montoro ◽  
Miguel Navarro-Alarcón ◽  
Triana Bergillos-Meca ◽  
Rafael Giménez-Martínez ◽  
Silvia Sánchez-Hernández ◽  
...  

2018 ◽  
Vol 26 (2) ◽  
pp. 307-328 ◽  
Author(s):  
Hesna Nursevin Öztop ◽  
Fatma Banu Çatmaz ◽  
Dursun Saraydin

Abstract Poly (methacrylamide / maleic acid) PM/MA and poly (methacrylamide) PM hydrogels were prepared aiming to be used as a support for invertase. Spectrophotometric, thermal analysis methods, swelling and diffusion experiments were used for the characterization of hydrogels. The swelling of PM/MA was higher than that of PM in water. The diffusion of water within the hydrogel was found to be non-Fickian. Invertase was immobilized onto PM and PM/MA (samples named PM-I and PM/MA-I respectively). The optimum pH values were found to be; 6.0, 5.0 and 5.5 for free invertase, PM-I and PM/MA-I respectively. The optimum temperature values were found to be 30 °C, 35 °C and 40 °C for free invertase, PM-I and PM/MA-I respectively. The Michaelis constant (Km) and maximum velocity of the enzymes (Vmax) were Km: 11,75 mM, Vmax: 1,95 μmol min−1 for free invertase, Km: 67,24 mM, Vmax: 60,6 μmol min−1 for PM-I and Km: 74,55 mM, Vmax: 18,12 μmol min−1 for PM/MA-I. PM/MA-I showed excellent thermal, operational and storage stability.


2012 ◽  
Vol 512-515 ◽  
pp. 2419-2423
Author(s):  
Yan Jun Wang ◽  
Shao Ling Zhuo ◽  
Sheng Chen

Chitosanase was immobilized on CSG hybrid material by cross-linking reaction and the immobilization conditions and characterization of the immobilized enzyme were carried out. The optimal conditions for immobilization were as follows: 0.1 g carrier material was treated with 2.5 ml 5% solution of glutaraldehyde and 2 ml chitosanase was immobilized on the carrier. Optimal temperature and pH for the immobilized enzyme were 60°C and 7.0, respectively. Kinetic parameter Km was10.64 g/l. The immobilized enzyme showed better operation and storage stability than the free enzyme.


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