• 제목/요약/키워드: Cheng Mingdao

검색결과 3건 처리시간 0.02초

정명도(程明道)의 인성론에 대한 연구

  • 조원일
    • 중국학논총
    • /
    • 제67호
    • /
    • pp.139-156
    • /
    • 2020
  • 程明道言性卽天道, 言人心之本體卽宇宙之本體, 道理雖至爲簡單, 但含義卻極爲豐富。我們可以一分解的程序步驟來言其奧蘊。首先, 本體卽於宇宙流行變化中見, 卽天道於宇宙流行變化中見。其次, 流行變化卽生生不已, 生生不已之機爲善, 故本體含善之價値性, 卽天道含善。最後, 本體在人爲性, 或天道賦於人爲性, 故人性亦含生生不已之機, 而人性爲善。而程明道說 "只此便是天地之化, 不可對此箇別有天地。天地的生化就表現在性體道德創造之純亦不已中。就此而言, 與程明道天人一本之主張並不相違背, 且可互爲補充證明, 在他的四維架構中, 這也是理論詮釋互相循環的一種模式。

정명도의 천도론(天道論)에 대한 연구

  • 조원일
    • 중국학논총
    • /
    • 제64호
    • /
    • pp.223-239
    • /
    • 2019
  • 程明道以天理言天道, 可細分爲天理之實說與天理之虛說. 天理之實說, 是就天理之超越本體自身言其內蘊, 稱之爲第一義之天理; 天理之虛說, 是就天理之自然之勢言其內蘊, 稱之爲第二義之天理. 一是超越性的萬物存在所以然之理, 一是現實上的萬物存在之然之理. 筆者以爲可以本體層與作用層來加以分疏. 前者是指天理超越之自體, 其至善,完美自足, 永恒而遍在; 後者是指天理作用於現象世界之表現, 天理內賦於萬事萬物, 就其現實存在而言, 一事有一事之理, 一物有一物之理, 但因事物之自然情勢各有不同, 故而在表現之理上亦各有不同, 在表現之理上雖各有不同, 但推其所以然之理, 則萬物皆不同. 因此, 此亦可理一分殊來作說明. 對於這些相關性的討論詮解, 如何予以連結溝通起來, 皆置於本文申論.

Screening, Gene Cloning, and Characterizations of an Acid-Stable α-Amylase

  • Liu, Xinyu;Jia, Wei;An, Yi;Cheng, Kun;Wang, Mingdao;Yang, Sen;Chen, Hongge
    • Journal of Microbiology and Biotechnology
    • /
    • 제25권6호
    • /
    • pp.828-836
    • /
    • 2015
  • Based on its α-amylase activity at pH 5.0 and optimal pH of the crude enzyme, a strain (named B-5) with acid α-amylase production was screened. The B-5 strain was identified as Bacillus amyloliquefaciens through morphological, physiological, and biochemical characteristics analysis, as well as 16S rDNA phylogenetic analysis. Its α-amylase gene of GenBank Accession No. GU318401 was cloned and expressed in Escherichia coli. The purified recombinant α-amylase AMY-Ba showed the optimal pH of 5.0, and was stable at a pH range of 4.0-6.0. When hydrolyzing soluble starch, amylose, and amylopectin, AMY-Ba released glucose and maltose as major end products. The α-amylase AMY-Ba in this work was different from the well-investigated J01542-type α-amylase which also came from B. amyloliquefaciens. AMY-Ba exhibited notable adsorption and hydrolysis ability towards various raw starches. Structure analysis of AMY-Ba suggested the presence of a new starch-binding domain at its C-terminal region.