Gl~~cinitr, the major sopbean glohrtlin, is ninrposed of scibunits having molecular weights of about 22,300 und 37.200. On the basis of umino acid analysis, the six subunits of glycinin isolated by isoelectric /Ociising ore all dijerent. The 'acidic' subunits have higher content of glutamic acid and proline. whereus the 'basic' sithiinits are higher in the h.vdrophohic amino acids bccine. tyrosine. phenylalanine, wline and cibnine.

Strawberry halves were infused with Valencia orange pectinmethylesterase (PME) under vacuum for 15 min at room temperature. Fruits were blotted onto pectin paper and stained for activity. Activity of PMEinfused fruit was about twice (0.36 unit/mL or 0.86 unit/mg protein) that of noninfused control (0.19 unit/mL) or water-infused control (0.16 unit/mL). Instron firmness values were not significantly different (P Յ Յ Յ Յ Յ 0.05) between noninfused and PME-infused fruit. Firmness of PME-infused fruit was about twice that of waterinfused control. Water-soluble pectin, chelator soluble pectin, alkaline soluble pectin, and total pectin ranged from 8.24 to 8.70, 3.24 to 4.56, 3.77 to 5.39, and 17.86 to 26.16 mg/100 mg alcohol insoluble solid (AIS), respectively, for all treatments.

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A protease. capuble of hydrolysing benzoyl DL-arginine p-nitroanilide (BAPA), and L-amino acid P-naphthylomide derivatives, was purified, by isoelectric focusing in the region pH 3 4 , from dormant and 6-day germinated soyabean seeds.The K, value using BAPA as wbsirate was found to be 5.03 X 1 0 -4~. Maximum activity of the enzyme towards BAPA was obtained in the p H 8.2-8.5 region. Slight activation was observed in the presence of 0.05 M concentration of CazT and Mg2-ions. The protease lacked caseinolytic activity, and was not inhibited by Kunitz soyabean irypsin inhibitor.The enzyme was focused at pH 4.80.

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