Lipolytic Enzyme Activity in Lysosomal Fraction from Porcine Muscle and Liver

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  • 豚筋肉および肝臓リソゾーム画分の脂質分解酵素活性について
  • ブタ キンニク オヨビ カンゾウ リソゾーム カクブン ノ シシツ ブンカイ

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Abstract

To determine the activity of lipolytic enzyme indigenous to meat, investigations were performed on lipolytic enzyme activity in porcine muscle and liver with natural fats and triglycerides as substrates. The porcine muscle and liver homogenates were fractionated by the procedures of differential centrifugation described by ONO and by SHIBKO and TAPPEL, respectively. The lysosomal (L) fraction possessed the highest specific activity of lipolytic enzyme in the subcellular fractions of muscle as well as in those of liver. The specific activity of the L fraction on olive oil was 6 times higher in liver than in muscle. The optimum pH for the enzyme activity of L fractions from muscle and liver was 4.5 with all of substrates used. The highest enzyme activity was observed at 50°C in both muscle and liver L fractions with olive oil and lard as substrates. Effects of inhibition or activation by the compounds used on the enzyme activity showed similarity between the enzymes from muscle and liver L fractions. The lipolytic enzyme in L fractions from muscle and liver hydrolyzed more rapidly triglycerides of unsaturated fatty acids than those of saturated fatty acids in the case of C18 acids. Although the rate of hydrolysis by L fraction was different in muscle from liver, the enzyme of the muscle L fraction hydrolyzed natural fats and triglycerides of higher fatty acids in a similar manner to that of the liver L fraction.

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