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- Pongsetkul, Jaksuma; Benjakul, Soottawat; Sumpavapol, Punnanee; Osako, Kazufumi; Faithong, Nandhsha
- Journal of food biochemistry 2017 v.41 no.1
- trypsin inhibitors, etc ; Acetes; Macrobrachium; actin; bacteria; chymotrypsin; condiments; fermentation; fluorides; hydrolysis; myosin heavy chains; oligopeptides; pH; palatability; proteolysis; raw materials; salting; shrimp; sodium chloride; soybeans; trypsin; Show all 21 Subjects
- ... Characteristics of endogenous proteases of shrimp, Acetes vulgaris (AP) and Macrobrachium lanchesteri (MP) as well as the changes in proteolytic activity during Kapi production were investigated. Maximal activity of AP and MP was found at pH 7, 60C and pH 8, 60C, respectively. Activity of both proteases decreased with increasing NaCl concentration (0–30%). Both extracts were strongly inhibited by ...
- Poonsin, Tanchanok; Sripokar, Pakteera; Benjakul, Soottawat; Simpson, Benjamin K.; Visessanguan, Wonnop; Klomklao, Sappasith
- Journal of food biochemistry 2017 v.41 no.2
- trypsin inhibitors, etc ; Thunnus alalunga; buffers; detergents; electrophoresis; fluorides; leather; molecular weight; pH; pollution; processing waste; proteolysis; silk; sodium chloride; sodium phosphate; soybeans; spleen; temperature; trypsin; tuna; Show all 20 Subjects
- ... This investigation aimed to characterize the proteinases and to study the effect of extraction media on proteinases recovery from albacore tuna spleen. Optimal activity of splenic extract was at pH 9.5 and 55°C. The enzyme was stable in a wide pH range of 6.0–10.0 but unstable at the temperatures greater than 50°C for 30–120 min. The proteolytic activity was strongly inhibited by soybean trypsin i ...