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This book systematically describes the green engineering, chemistry and manufacture of bio-based polymers and composites derived from plants. This book gives a thorough introduction to bio-based material resources, availability, sustainability, bio-based polymer formation, extraction and refining technologies, and the need for integrated research and multi-disciplinary working teams. It provides an in-depth description of adhesives, resins, plastics, and composites derived from plant oils, proteins, starches, and natural fibers in terms of structures, properties, manufacturing, and product performance. This is an excellent book for scientists, engineers, graduate students and industrial researchers in the field of bio-based materials.

Progress in the biological and microbiological sciences involved in the manufacture of fermented foods has led to commercialization and heightened interest among scientists and food processors. This up-to-date reference explores the history, microorganisms, quality assurance, and manufacture of fermented food products derived from plant sources. The book describes fermented food flavors, manufacturing, and biopreservation, and supplies a detailed exploration of a range of products derived from soy, fruit, vegetables, and cereals. It also explores various specialty products, including balsamic vinegar and coconut milk, and examines ingredients such as proteolytic bacteria, enzymes, and probiotics.

In laboratory animals, the consumption of soy protein, rather than animal protein, decreases serum cholesterol concentrations, but studies in humans have been inconclusive. In this meta-analysis of 38 controlled clinical trials, we examined the relation between soy protein consumption and serum lipid concentrations in humans. Methods. We used a random-effects model to quantify the average effects of soy protein intake on serum lipids in the studies we examined and used hierarchical mixed-effects regression models to predict variation as a function of the characteristics of the studies. Results. In most of the studies, the intake of energy, fat, saturated fat, and cholesterol was similar when the subjects ingested control and soy-containing diets; soy protein intake averaged 47 g per day. Ingestion of soy protein was associated with the following net changes in serum lipid concentrations from the concentrations reached with the control diet: total cholesterol, a decrease of 23.2 mg per deciliter (0.60 mmol per liter; 95 percent confidence interval, 13.5 to 32.9 mg per deciliter [0.35 to 0.85 mmol per liter]), or 9.3 percent; low-density lipoprotein (LDL) cholesterol, a decrease of 21.7 mg per deciliter (0.56 mmol per liter; 95 percent confidence interval, 11.2 to 31.7 mg per deciliter [0.30 to 0.82 mmol per liter]), or 12.9 percent; and triglycerides, a decrease of 13.3 mg per deciliter (0.15 mmol per liter; 95 percent confidence interval, 0.3 to 25.7 mg per deciliter [0.003 to 0.29 mmol per liter]), or 10.5 percent. The changes in serum cholesterol and LDL cholesterol concentrations were directly related to the initial serum cholesterol concentration (P 0.001) The ingestion of soy protein was associated with a nonsignificant 2.4 percent increase in serum concentrations of high-density lipoprotein (HDL) cholesterol. Conclusions. We found that the consumption of soy protein rather than animal protein significantly decreased serum concentrations of total cholesterol

Protein-polysaccharide conjugates were generally prepared by dry-heating. However, it was time-consuming and the sample gained was inhomogeneous. A faster way of preparing protein-polysaccharide conjugates is needed. Accordingly, soy protein isolates (SPI)-acacia gum (GA) conjugates prepared by the wet-heating method were studied in the present work. Physicochemical properties of SPI-GA conjugates were also determined. The results showed that the wet-heating method could improve the rate of the graft reaction of protein and polysaccharide. The solubility of SPI-GA conjugates was significantly higher than that of unreacted SPI-GA mixtures and SPI at the same pH values. The emulsion activity index of the grafted SPI increased remarkably. Moreover, a significant improvement of the emulsifying stability index was observed and emulsions with a smaller droplet size were obtained. No visible flocculation during extended storage (30 days) was observed. The time course of the development of the graft reaction of SPI with GA was also shown by SDS-PAGE.

The search for new value-added uses for oilseed and animal proteins led us to develop protein-based wood adhesives. Low-fat soy and peanut flours and blood meal were hydrolyzed in an alkaline state, and PF-cross-linked protein resins were formulated by reacting the protein hydrolyzates with phenol-formaldehyde (PF) in solid-tosolid ratios ranging from 70% to 50% hydrolyzates and 30% to 50% PF. Physical properties of medium density fiberboard (MDF) bonded with protein-based phenolic resins were compared to those of boards bonded with ureaformaldehyde (UF) and PF resins, and flakeboard bonded with soy protein-based phenolic resin was compared to PF-bonded board. As MDF binders, adhesive properties of protein-based phenolic resins depended upon protein content of proteinacious materials. MDF board bonded with blood-based phenolic resin was comparable to PF-bonded board and met the requirements for exterior MDF. Boards bonded with soy-protein-based phenolic resin met requirements for interior MDF, while peanut-based phenolic failed to meet some of the requirements. Flakeboard bonded with soy-protein-based phenolic resins was inferior to PF-bonded board but outperformed PF-bonded board in accelerated aging tests. Although they exhibit a slow curing rate, the cost effectiveness and superior dimensional stability of protein-based phenolic resins may make them attractive for some uses.

We determine the effects of the technology of obtaining potato protein preparation and of different variants of enzymatic hydrolysis on the chemical and amino acid compositions of the hydrolysates obtained. Potato protein concentrates obtained through their thermal coagulation in potato juice with calcium chloride, calcium lactate or without salt addition were subjected to enzymatic hydrolysis using two commercial hydrolytic enzymes: endopeptidase (Alcalase) and exopeptidase (Flavourzyme). Chemical (contents of ash, total and coagulable protein) and amino acid compositions of the hydrolysates obtained were determined. On the ground of the findings it was stated that the type of potato protein preparation used and conditions of enzymatic modification influenced on the properties of the hydrolysates obtained. Preparations obtained during the study were characterised by similar chemical and amino acid compositions, whereas the preparation obtained through thermal coagulation with the use of calcium lactate contained insignificantly more protein and essential amino acids. The least liable to enzymatic hydrolysis was the preparation obtained by using calcium chloride, particularly when only endopeptidase was used. The application of endopeptidase enzyme enabled to obtain 60% of proteolysis efficiency and the addition of the second enzyme (exopeptidase) to the protein solution insignificantly increased the proteolysis efficiency (to ca 70%), mainly when the preparation coagulated with the use of calcium chloride was hydrolysed. Proteolysis of the protein preparations obtained with the use of two enzymes was more favourable, particularly due to the quantity of free amino acids in and amino acids composition of the hydrolysates.

Expansins are proteins that induce extension in isolated plant cell walls in vitro and have been proposed to disrupt noncovalent interactions between hemicellulose and cellulose microfibrils. Because the plant primary cell wall acts as a constraint to cell enlargement, this process may be integral to plant cell expansion, and studies of expansins hew focused on their role in growth. We report the identification of an expansin (LeExp1) from tomato that exhibits high levels of mRNA abundance and is specifically expressed in ripening fruit, a developmental period when growth has ceased but when selective disassembly of cell wall components is pronounced. cDNAs closely related to LeExp1 were also identified in ripening melons and strawberries, suggesting that they are a common feature of fruit undergoing rapid softening. Furthermore the sequence of LeExp1 and its homologs from other ripening fruit define a subclass of expansin genes. Expression of LeExp1 is regulated by ethylene, a hormone known to coordinate and induce ripening in many species. LeExp1 is differentially expressed in the ripening-impaired tomato mutants Nr, rin, and nor, and mRNA abundance appears to be influenced directly by ethylene and by a developmentally modulated transduction pathway. The identification of a ripening-regulated expansin gene in tomato and other fruit suggests that, in addition to their role in facilitating the expansion of plant cells, expansins may also contribute to cell wall disassembly in nongrowing tissues, possibly by enhancing the accessibility of noncovalently bound polymers to endogenous enzymic action

The sos1 mutant of Arabidopsis thaliana is more than 20 times more sensitive to NaCl stress than wild-type Arabidopsis. Because proline (Pro) is generally thought to have an important role in plant salt tolerance, the sos1 mutant and the wild type were compared with respect to their capacity to accumulate Pro under NaCl stress, and sos1 mutant plants accumulated more Pro than the wild type. The P5CS gene, which catalyzes the rate-limiting step in Pro biosynthesis, is induced by salt stress to a higher level in sos1 than in the wild type. Although a defective high-affinity K uptake system in sos1 causes K deficiency and inhibits growth in NaCl-treated plants, this decrease is not a sufficient signal for Pro accumulation and P5CS gene expression. Not all salt-stress-induced genes have a higher level of expression in sos1. The expression levels of AtPLC and RD29A, which encode a phospholipase C homolog and a putative protective protein, respectively, are the same in sos1 as in the wild type. However, the expression of AtMYB, which encodes a putative transcriptional factor, is induced to a much higher level by salt stress in sos1. Thus, the SOS1 gene product serves as a negative regulator for the expression of P5CS and AtMYB, but has no effect on AtPLC and RD29A expression