Chemical Modification of Amino Groups in Mucor miehei Aspartyl Proteinase, Porcing Pepsin, and Chymosin : I. Structure and Function(Food & Nutrition)

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概要

• 論文の詳細を見る

• The effects of chemical modification of g-amino groups (using the water soluble polyanionic copolymer ethylene/maleic anhydride) on the structure and function of various aspartyl proteinases (the proteinase from the fungus Mucor miehei (MMP), and the mammalian proteinases porcine pepsin and chymosin) were examined. Modification of 100% of the lysyl residues in the proteinases resulted in an increased milk-clotting to proteolytic activity ratio (MC/PA) for pepsin and chymosin, and a lower MC/PA for MMP. Amino-modified MMP was insensitive to the proteinase inhibitor pepstatin, but modified pepsin and chymosin were inactivated. Modification shifted the pH-activity optimum of the mammalian enzymes by 0.5 pH units to a more alkaline pH and to a more acidic optimum for MMP. Amino modification also decreased the thermostability of the fungal enzyme, Changes in tertiary structure and significant differences in the proportions of the secondary structure fractions α-helix and β-sheet were evident only for modified MMP. Results from this study suggested that MMP was more susceptible to destabilization by charge alteration than aspartyl proteinases of mammalian origin.

• 社団法人日本農芸化学会の論文
• 1991-08-23

著者

• Yada R

  Univ. Guelph Ontario Can

• Yada Rickey

  Department Of Food Science Ontario Agricultural College University Of Guelph

• Billings Gail

  Department Of Food Science University Of Guelph

• Smith Jeff

  Department Of Food Science University Of Guelph

関連論文

• Purification of Two Fungal Aspartic Proteinases Using Fast Protein Liquid Chromatography(Food & Nutrition)
• Physico-chemical Properties of Purified Isoforms of the 12S Seed Globulin from Mustard Seed (Brassica alba)
• Isolation, Purification, and Characterization of the Oligomeric Seed Globulin from Amaranthus hypochondriacus(Biological Chemistry)
• Chemical Modification of Amino Groups in Mucor miehei Aspartyl Proteinase, Porcine Pepsin, and Chymosin : II. Conformational Stability(Food & Nutrition)
• Chemical Modification of Amino Groups in Mucor miehei Aspartyl Proteinase, Porcing Pepsin, and Chymosin : I. Structure and Function(Food & Nutrition)

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