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( Chaeri Park ),( Yun-kyoung Song ),( Young-hyun Kim ),( Yena Jung ),( Young-ho Park ),( Bong-seok Song ),( Taekil Eom ),( Ju-sung Kim ),( Sang-hyun Kim ),( Ji-su Kim ),( Sun-uk Kim ),( Sang-rae Lee ) 한국미생물생명공학회(구 한국산업미생물학회) 2019 Journal of microbiology and biotechnology Vol.29 No.8
Hyaluronidases enhance therapeutic drug transport by breaking down the hyaluronan barrier to lymphatic and capillary vessels, facilitating their tissue absorption. Commercially available hyaluronidases are bovine in origin; however, they pose risks such as bovine spongiform encephalopathy. The present study aimed to develop a novel, highly active hyaluronidase and assess its function. Therefore, in order to find the most efficient active hyaluronidase, we produced several shortened hyaluronidases with partial removal of the N- or C-terminal regions. Moreover, we created an enzyme that connected six histidines onto the end of the hyaluronidase C-terminus. This simplified subsequent purification using Ni<sup>2+</sup> affinity chromatography, making it feasible to industrialize this highly active recombinant hyaluronidase which exhibited catalytic activity equal to that of the commercial enzyme. Therefore, this simple and effective isolation method could increase the availability of recombinant hyaluronidase for research and clinical purposes.
( Chaeri Park ),( Young-hyun Kim ),( Sang-rae Lee ),( Soojin Park ),( Yena Jung ),( Youngjeon Lee ),( Ji-su Kim ),( Taekil Eom ),( Ju-sung Kim ),( Dong-mok Lee ),( Bong-suk Song ),( Bo-woong Sim ),( S 한국미생물생명공학회(구 한국산업미생물학회) 2018 Journal of microbiology and biotechnology Vol.28 No.9
Hyaluronidases are a family of enzymes that catalyse the breakdown of hyaluronic acid, which is abundant in the extracellular matrix and cumulus oocyte complex. To investigate the activity of recombinant bovine sperm hyaluronidase 1 (SPAM1) and determine the effect of the Asn-X-Ser/Thr motif on its activity, the bovine SPAM1 open reading frame was cloned into the mammalian expression vector pCXN2 and then transfected to the HEK293 cell line. Expression of recombinant bovine hyaluronidase was estimated using a hyaluronidase activity assay with gel electrophoresis. Recombinant hyaluronidase could resolve highly polymeric hyaluronic acid and also caused dispersal of the cumulus cell layer. Comparative analysis with respect to enzyme activity was carried out for the glycosylated and deglycosylated bovine sperm hyaluronidase by N-glycosidase F treatment. Finally, mutagenesis analysis revealed that among the five potential N-linked glycosylation sites, only three contributed to significant inhibition of hyaluronic activity. Recombinant bovine SPAM1 has hyaluronan degradation and cumulus oocyte complex dispersion ability, and the N-linked oligosaccharides are important for enzyme activity, providing a foundation for the commercialization of hyaluronidase.
Characterization and Biochemical properties of water soluble quercetin in steviol glucosides
Thi Thanh Hanh NGUYEN,ChangSeop SEO,Namhyeon PARK,Jungmin HA,DongGu LEE,Songhee HAN,Tae-kyung LEE,Jaewon HUR,Chaeri SONG,Shina JIN,So-hyung KWAK,Jeesoo KIM,Jinbeom SI,Doman KIM 한국생물공학회 2016 한국생물공학회 학술대회 Vol.2016 No.10
Yu, Shin-Hye,Kwak, So-Hyung,Nguyen, Thi Thanh Hanh,Seo, Ye-Seul,Song, Chaeri,Mok, Il Kyoon,Kim, Doman Springer Netherlands 2018 Biotechnology letters Vol.40 No.2
<P><B>Objectives</B></P><P>To develop preventive canine oral health bio-materials consisting of probiotics and glucanase to reduce insoluble glucan and volatile sulfur compound formation.</P><P><B>Results</B></P><P>Co-cultivation of <I>Enterococcus faecium</I> T7 with <I>Streptococcus mutans</I> at inoculation ratio of 3:1 (v/v) resulted in 25% reduction in the growth of <I>Streptococcus mutans</I>. Amounts of soluble and insoluble glucans produced by <I>S. mutans</I> were decreased to 70 and 55%, respectively. Insoluble glucan was decreased from 0.6 µg/ml in <I>S. mutans</I> culture to 0.03 µg/ml in <I>S. mutans</I> co-cultivated with <I>E. faecium</I> T7 in the presence of <I>Lipomyces starkeyi</I> glucanase. Volatile sulfur compound, a main component of halitosis produced by <I>Fusobacteria nucleatum</I>, was decreased by co-cultivating <I>F. nucleatum</I> with <I>E. faecium.</I></P><P><B>Conclusion</B></P><P><I>E. faecium</I> and glucanase can be combined as potentially active ingredients of oral care products for pets by reducing plaque-forming bacteria growth and their by-products that cause cavity and periodontal disease.</P><P><B>Electronic supplementary material</B></P><P>The online version of this article (10.1007/s10529-017-2478-z) contains supplementary material, which is available to authorized users.</P>