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Cloning and Expression of Schwanniomyces castellii Starch Gene (Schwanniomyces castellii 전분 유전자의 Cloning과 발현)

  • Park, Jong-Chun;Bai, Suk;Chun, Soon-Bai
    • Microbiology and Biotechnology Letters
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    • v.18 no.6
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    • pp.653-659
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    • 1990

  • The gene encoding glucoamylase from Schwanniomyces cagtellii CBS 2863 was cloned and expressed in Saccharomyces cerevisiae. Southern blot analysis confirmed that this glucoamylase gene was derived from the genomic DNA of Schwanniomyces ccastellii and that no DNA fragments corresponding to 5.1 or 1.3 kb of Sch. casteltii DNA were detected in S. cereuisiae. The glucoamylase activity from S. cerevisiae transformant was approximately 2,000 times less than that of donor yeast. No expression was found in E. coti. The secreted glucoamylase from S. cerevisiae transformant was indistinguishable from that of Sch. eastellii on the basis of molecular weight and enzyme properties.

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Saprolegnia ferax에 의한$\beta$-amylase의 생산 및 특성

  • Bai, Suk;Cho, Nam-Chul;Chun, Soon-Bai
    • Microbiology and Biotechnology Letters
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    • v.25 no.2
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    • pp.109-114
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    • 1997

  • The Oomycete Saprolegnia ferax produces an extracellular $\beta$-amylase, Maximum enzyme yield was attained after 7 days of growth in YNB starch medium (pH 6.5) at 25$\circ$C. The amylase was pu- rified 24-fold by ultrafitration, HPLC DEAE column and HPLC gel filtration. The purfied enzyme was a monomeric glycoprotein with a molecular weight of about 44,000 dalton. The pH and temperature optima were 6.5 and 50$\circ$C, respectively. The enzyme was fairly stable up to 50$\circ$C and at acidic pH region (pH 4.0-7.0). The apparent Km and Vmax values of the enzyme against soluble starch were 0.77 mg/ml and 2,174 $\mu$moles/mg protein, respectively. Amino acid analysis indicated that the enzyme was enriched in alanine, glycine, leucine and acidic amino acid. Starch hydrolysis with the enzyme released maltose but not glucose, whereas maltotriose, Schardinger dextrin ($\alpha$-cyclodextrin) and pullulan were not hydrolysed by the enzyme. The enzyme was inhibited by Schardinger dextrin, p-chloromercuribenzoate(PCMB), CU$^{2+}$' and Hg$^{2+}$. Inhibition of the enzyme by PCMB could be reversed by the addition of cysteine and mercaptoethanol.

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Effectiveness of Oral Glycopyrrolate Use in Compensatory Hyperhidrosis Patients

  • Gong, Tai Kyung;Kim, Do Wan
    • The Korean Journal of Pain
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    • v.26 no.1
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    • pp.89-93
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    • 2013

  • Compensatory hyperhidrosis or reflex hyperhidrosis is the increase in sweating in the postoperative stage of thoracic sympathectomy or lumbar sympathectomy. It shares several features with anxiety disorders and has a negative impact on a patient's quality of life. Oralglycopyrrolate is one of the treatment options available. This study reviewed case notes in a series of 19 patients with compensatory hyperhidrosis. We made a comparison between the Milanez de Campos score of a pre-glycopyrrolate medication group and the Milanez de Campos score of a post-glycopyrrolate medication group. The Beck Depression Inventory (BDI) score, Beck Anxiety Inventory (BAI) score, and autonomic nervous system (ANS) scale score were also compared between the pre-medication and post-medication groups. In the post-glycopyrrolate medication group, there was decrease in the Milanez de Campos score, BAI score, and BDI score (P < 0.05). But no meaningful change was seen in the ANS score in the post-glycopyrrolate medication group (P > 0.05). Glycopyrrolate is an effective medication in the treatment of compensatory hyperhidrosis that, can alleviate anxiety and improve patients' quality of life.

  • https://doi.org/10.3344/kjp.2013.26.1.89 인용 PDF KSCI