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Effect of Thermal Treatment on the Texture and Microstructure of Abalone Muscle (Haliotis discus)
Beiwei Zhu,Xiuping Dong,Liming Sun,Guihua Xiao,Xuejiao Chen,Yoshiyuki Murata,Chenxu Yu 한국식품과학회 2011 Food Science and Biotechnology Vol.20 No.6
The texture and microstructure of edible abalone meats were studied during heat treatments from 50to 100^oC for 60 min. No increase in extractable soluble collagen content was observed below 80^oC, but a 9-fold increase was observed at 100^oC. SDS-PAGE showed that extractable myosin heavy chains and paramyosin contents reduced significantly at 80^oC, and disappeared completely at 100^oC. The shear force increased slowly from 50 to 70^oC, but relaxed back to the initial level at 100^oC. Rapid reduction of hardness was observed at 50^oC, minimum hardness was obtained at 100^oC. Springness, cohesiveness,chewiness, and resilience were enhanced to maximum levels at 70, 90, 70, and 90^oC, respectively. Optical micrographs and transmission electron microscope showed a significant increase of intermyofibrillar gaps at 90^oC and broken fibers at 100^oC. Results suggested that 80^oC might be a suitable temperature to produce ready-to-eat abalone products.
Changes of Collagen in Sea Cucumber (Stichopus japonicas) During Cooking
Xiuping Dong,Beiwei Zhu,Liming Sun,Jie Zheng,Dan Jiang,Dayong Zhou,Haitao Wu,Yoshiyuki Murata 한국식품과학회 2011 Food Science and Biotechnology Vol.20 No.4
Changes of the collagen in sea cucumber (Stichopus japonicas) during cooking were investigated. Crude collagen fibers (CCF) is more sensitive to heat than pepsin-solubilized collagen (PSC), absorbance at 226-232nm increased from 60 to 100^oC. PSC nearly completely degraded after cooking for 8-10 h, 4-6 h, 1-1.5 h, 40-50 min, and 10-20 min at 60, 70, 80, 90, and 100^oC,respectively. Collagen fiber shrinkage, disappearance of periodic cross striation, complete denaturation, and dispersion of denatured fibers at 40, 60, 80 and 100^oC,respectively, were demonstrated by transmission electron microscope (TEM). Above results might be instructional for sea cucumber processing and collagen usage.
Effect of Matrix Metalloproteinase on Autolysis of Sea Cucumber Stichopus japonicus
Li-Ming Sun,Ting-Ting Wang,Bei-Wei Zhu,Hai-Ling Niu,Rui Zhang,Hong-Man Hou,Gong-Liang Zhang,Yoshiyuki Murata 한국식품과학회 2013 Food Science and Biotechnology Vol.22 No.5
To investigate the relationship between matrix metalloproteinase (MMPs) and autolysis of sea cucumber Stichopus japonicus, the dermis homogenate was incubated at 25oC to induce autolysis. EDTA Na2 and 1,10-phenanthroline were used to verify the effect of MMPs on autolysis, which was measured by soluble protein and protein pattern. Soluble protein level increased during a 6-h autolysis process. SDS-PAGE demonstrated obvious protein degradation with the concomitant occurrence of degradation products. The above two indicators could be inhibited significantly by EDTA Na2 and 1,10-phenanthroline, indicating that MMPs might play a significant role in autolysis of sea cucumber.
Li-Ming Sun,Bei-Wei Zhu,Hai-tao Wu,Lei Yu,Da-Yong Zhou,Xiuping Dong,Jing-Feng Yang,Dong-Mei Li,Wen-Xiu Ye,Yoshiyuki Murata 한국식품과학회 2011 Food Science and Biotechnology Vol.20 No.4
Cathepsin B from the gut of sea cucumber (Stichopus japonicas) was purified 81-fold with a 3%recovery by ammonium sulfate fractionation and a series chromatography on DEAE Sepharose CL-6B, Sephadex G-75, and TSK-Gel 3000 SWxl. The purified protein appeared as a single band on Native-PAGE but showed 2bands of 23 and 26 kDa on SDS-PAGE. The optimum activity was found at pH 5.5 and 45°C. The enzyme was stable at pH 4.5-6.0 and the thermal stability was up to 50oC. The enzyme was strongly inhibited by E-64, iodoacetic acid, and antipain, demonstrating it is a cysteine protease containing sulfhydryl groups. Cu^2+, Ni^2+, and Zn^2+ could strongly inhibit the enzyme activity. The amino acid sequences of the purified enzyme were acquired by mass spectrometer, which did not show any homology with previously described cathepsins, suggesting it may be a novel member.
MPK9 and MPK12 function in SA-induced stomatal closure in <i>Arabidopsis thaliana</i>
Khokon, Md. Atiqur Rahman,Salam, Mohammad Abdus,Jammes, Fabien,Ye, Wenxiu,Hossain, Mohammad Anowar,Okuma, Eiji,Nakamura, Yoshimasa,Mori, Izumi C.,Kwak, June M.,Murata, Yoshiyuki Informa UK (TaylorFrancis) 2017 Bioscience, Biotechnology, and Biochemistry Vol.81 No.7
<P>Salicylic acid (SA) induces stomatal closure sharing several components with abscisic acid (ABA) and methyl jasmonate (MeJA) signaling. We have previously shown that two guard cell-preferential mitogen-activated protein kinases (MAPKs), MPK9 and MPK12, positively regulate ABA signaling and MeJA signaling in Arabidopsis thaliana. In this study, we examined whether these two MAPKs are involved in SA-induced stomatal closure using genetic mutants and a pharmacological, MAPKK inhibitor. Salicylic acid induced stomatal closure in mpk9 and mpk12 single mutants but not in mpk9 mpk12 double mutants. The MAPKK inhibitor PD98059 inhibited SA-induced stomatal closure in wild-type plants. Salicylic acid induced extracellular reactive oxygen species (ROS) production, intracellular ROS accumulation, and cytosolic alkalization in the mpk9, mpk12, and mpk9 mpk12 mutants. Moreover, SA-activated S-type anion channels in guard cells of wild-type plants but not in guard cells of mpk9 mpk12 double mutants. These results imply that MPK9 and MPK12 are positive regulators of SA signaling in Arabidopsis guard cells.</P>