The effects of hydrothermal cooking (HTC) at alkaline conditions on refunctionalization of heat-denatured protein of extruded-expelled (EE) soy meals and on preparation of soy protein isolate (SPI) from EE soy meal were determined. Two HTC setups, flashing-out HTC (without holding period) and HTC with holding for 42 s at 154°C, were evaluated. Alkali (NaOH) addition dramatically enhanced the refunctionalization of EE meal having an initial protein dispersibility index of 35. The more alkali added, the more refunctionalization occurred. Extensive refunctionalization was achieved at 0.6 mmol alkali/g EE meal, and additional improvement was small with more alkali. For both HTC setups, the solids and protein yields of SPI from alkali-HTCtreated EE meals were significantly higher than those from HTC without alkali addition. The yield of protein as SPI increased from 40 to 82% after HTC treatment at 0.6 mmol alkali/g EE meal compared with no alkali addition. The emulsification capacities of SPI after alkali-HTC were similar to those from HTC without alkali. SPI from holding-tube HTC-treated EE meals had higher emulsification capacities than those prepared by flashing-out HTC.Paper no. J11081 in JAOCS 82, 451-456 (June 2005).The use of soy protein ingredients by the food industry is increasing rapidly owing to health benefits, low cost, and versatile functionalities. Most soy protein products are manufactured from highly soluble (flash-desolventized) hexane-defatted soybean meal. Solvent extraction is capital intensive and unsuitable for processing small amounts of identity-preserved soybeans. Extrusion-expelling (EE) is a promising technique that presses the oil from the whole or cracked seeds and is suitable for processing small lots of identity-preserved seeds (1,2). EE differs from traditional screw pressing in that a dry extruder replaces steam-heated stack cookers or rotary dryers. Compared with solvent-extracted white flakes, EE protein meals that are processed into EE soy flour have much more heat exposure and protein denaturation [15-60 vs. 80-90 protein dispersibility index (PDI)], contain significantly more residual oil (6-12 vs. 1%), have lower levels of heat-sensitive antinutritional factors (trypsin inhibitors) and enzymes (such as lipoxygenase), and possess a pleasant nutty flavor. Typical EE meal contains 50% protein and 6% oil, and 90% of its trypsin inhibitors are inactivated (1). The use of protein ingredients prepared from EE meal in foods, however, is limited by their poor functional properties and low yields of soy protein isolate (SPI), a direct consequence of heat denaturation of the protein.Our previous work showed that SPI could be prepared from EE meals; however, the yields were low (the SPI and protein yields were only 25 and 40%, respectively) (6). Inspired by the work of Johnson (3) and Wang and Johnson (4), we demonstrated that hydrothermal cooking (HTC) could be used to refunctionalize heat-denatured proteins of EE meals (5). We also demonstrated the feasibility of using HTC as a pretreat...