Lysinoalanine, N6-(DL-2-amino-2-carboxyethyl)-L-lysine, an unusual amino acid implicated as a renal toxic factor in rats, has been found in proteins of home-cooked and commercial foods and ingredients. Although it has been reported to occur in both edible and nonfood proteins only after alkali treatment, it has now been identified in food proteins that had not been subjected to alkali. Lysinoalanine is generated in a variety of proteins when heated under nonalkaline conditions.

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The functional and nutritional properties of a bland, light colored corn protein concentrate (MCPC) have been investigated. This material contains 67% protein (dsb) and less than 0.5% fat. The water solubility is low, but water and fat binding properties are similar to those of a commercial soy concentrate. MCPC is rich in methionine and cystine, and forms complementary protein mixtures having enhanced nutritive value with soy products. The PER of a 20/80 (protein basis) mixture of MCPC and soy concentrate was found to be 86% the value for casein compared to 73% of the casein value for soy concentrate alone. Digestibility (in vitro) of MCPC was 0.82.

The heat stability of a bacterial α‐amylase is important for industrial starch utilization. Although extensive studies have been done on heat stable α‐amylase from various bacterial species little is known about the α‐amylases of Bacillus licheniformis. In order to get better understanding of thermostable amylases produced by different strains of B. licheniformis and provide information how to utilize the enzyme in starch processing, studies on purification and characterization of a commercial heat stable bacterial α‐amylase from B. licheniformis BLM 1777 are reported.

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