Authors: Zhi Jiang Li Sang Moo Kim
Publish Date: 2013/01/11
Volume: 169, Issue: 4, Pages: 1386-1396
Abstract
Hatching enzyme HE is of importance to degrade egg membrane to let the larvae be free HE was purified and characterized from starfish blastula The specific activity and the purification ratio of the purified HE with 1109 kDa of molecular weight were 44962 U/mg and 742fold respectively Its optimal pH and temperature for activity were pH 80 and 30 °C respectively This enzyme was relatively stable in the range of pH 40–60 and 30–40 °C This enzyme was inhibited by ethylene diamine tetraacetic acid EDTA and ethylene glycol tetraacetic acid and also done moderately by Leupeptin tosyllysine chloromethyl ketone tosylphenylalanine chloromethyl ketone and phenylmethanesulfonyl fluoride Zn2+ ion activated HE activity strongly and recovered the EDTApretreated activity more than did Ca2+ Mg2+ and Cu2+ Based on the results above the starfish HE was classified as a zinc metallo and trypsinlike serine protease The values of Km Vmax and Kcat of the starfish HE on dimethyl casein were 031 mg/ml 017 U/ml and 12270 s−1 respectively whereas 109 mg/ml 012 U/ml and 77198 s−1 on type I collagen Therefore the starfish HE could be a potential cosmeceutical because of its strong cleavage specificity on type I collagenThis work was supported by grant no RTI 050102 from the Regional Technology Innovation Program of the Ministry of Knowledge Economics MKE Republic of Korea Zhi Jiang Li is a recipient of a graduate fellowship provided by Brain Korea BK21 program sponsored by the Ministry of Education Science and Technology Republic of Korea
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